Structures and biological functions of IL-31 and IL-31 receptors

86Plant Signaling & Behavior2009; Vol. 4 Issue 2of protein-DNA interaction is affected by sequences located at the N-terminal of the HD-Zip I proteins.5HD-Zip class II is composed of nine members (ATHB2/HAT4, ATHB4, HAT1-HAT3, HAT9, HAT14, HAT17 and HAT22) in Arabidopsis. All these members are characterized by the presence of a third domain, known as CPSCE, located downstream of the Zip motif and involved in cellular redox status perception.6 HD-ZipII proteins are able to recognized DNA regions with the pseudopalindromic sequence CAAT(C/G)ATTG. Only five members are included in the HD-Zip class III in Arabidopsis (ATHB8, PHAVOLUTA /ATHB9, PHABULOSA /ATHB14, CORONA /ATHB15 and REVOLUTA /IFL1). Members of this group also share three additional domains: a MEKHLA domain possibly involved in oxygen redox and light signaling,7 a START domain motif with putative lipid binding capability,8 and a SAD domain which is a transcriptional activation domain.9 In vitro experiments have shown that, ATHB9, a member of this class, has high affinity for the pseudopalindromic sequence GTAAT(G/C)ATTAC.10HD-ZipIV comprises sixteen members in Arabidopsis includingGLABRA 2.1 Despite lacking a MEKHLA domain, members of this group have a START and SAD motifs. HD-Zip IV proteins targetthe sequence which is characterized by TAAA core.11Biological Functions of HD-Zip ProteinsMembers of HD-Zip class I are generally involved in abiotic stress responses such as water and light stress 12,13 Expression studies reveal that ATHB12 and ATHB7 are upregulated by water-limiting conditions and applications of ABA.14 ATHB6, another member of this class is a crucial regulator in the ABA signal pathway possibly by interacting with ABI1.15 Evidences that HD-Zip class I proteins might be implicated in ABA responses have also been shown in Picea glauca (white spruce) where PgHZ1 increases ABA sensitivity and promotes embryogenesis in vitro.16 Other members of this class, including ATHB52, are affected by light conditions and play a key role during photomorphogenesis and de-etiolation.17Proteins of class II are mainly involved in phototropism and auxin responses as revealed by expression and transformation studies.18In Arabidopsis shade avoidance response is regulated by ATHB-2 through complex mechanisms involving three distinct phytochromes. Hypocotyl elongation, similar to that observed in wild type plantsgrown under far red light conditions, was induced in Arabidopsisseedlings overexpressing ATHB-2. By contrast an opposite phenotype[Plant Signaling & Behavior 4:2, 86-88; February 2009]; ©2009 Landes BioscienceHomeodomain-leucine zipper (HD-Zip) proteins are transcrip-tion factors unique to plants and are encoded by more than 25 genes in Arabidopsis thaliana . Based on sequence analyses these proteins have been classified into four distinct groups: HD-Zip I–IV . HD-Zip proteins are characterized by the presence of two functional domains; a homeodomain (HD) responsible for DNA binding and a leucine zipper domain (Zip) located immediately C-terminal to the homeodomain and involved in protein-protein interaction. Despite sequence similarities HD-ZIP proteins partici-pate in a variety of processes during plant growth and development. HD-Zip I proteins are generally involved in responses related to abiotic stress, abscisic acid (ABA), blue light, de-etiolation and embryogenesis. HD-Zip II proteins participate in light response, shade avoidance and auxin signalling. Members of the third group (HD-Zip III) control embryogenesis, leaf polarity, lateral organ initiation and meristem function. HD-Zip IV proteins play signifi-cant roles during anthocyanin accumulation, differentiation of epidermal cells, trichome formation and root development.Structure of HD-Zip Proteins Homeodomain leucine zipper (HD-Zip) proteins are transcription factors classified into four different groups based on gene structure, presence of unique domains and function.1 Unique features of allHD-Zip members are the presence of a homeodomain (HD) and a leucine zipper motif (Zip). The HD domain is involved in DNA binding whereas the Zip domain is involved in protein homo and heterodimerization.2 Functional studies using truncated proteins have shown the requirement of the Zip motif for the DNA binding ability of the HD domain.3In Arabidopsis the HD-Zip class I comprises seventeen members encoding proteins of similar size (~35 kDa) including a well conserved HD domain and a less conserved Zip motif. PCR-assisted binding site selection and footprinting assays showed the ability of HD-Zip I proteins to recognize and bind the pseudopalindromic sequence CAAT(A/T)ATTG.4 The affinity, but not the specificity, Mini-ReviewStructure and function of homodomain-leucine zipper (HD-Zip) proteinsMohamed Elhiti and Claudio Stasolla*Department of Plant Science; Faculty of Agriculture and Food Sciences; University of Manitoba; Manitoba, CanadaAbbreviation: HD-Zip, homeodomain-leucine zipper; ABA, abssisic acid; SAM, shoot apical meristem Key words: homeodomain-leucine zipper, development, structure, function, signaling, embryogenesis*Correspondence to: Claudio Stasolla; Department of Plant Science; Faculty ofAgriculture and Food Sciences; University of Manitoba; Manitoba R3T2N2 Canada;Tel.:204.474.6098;Fax:204.474.7528;Email:*********************.caSubmitted: 12/19/08; Accepted: 12/23/08Previously published online as a Plant Signaling & Behavior E-publication: /journals/psb/article/7692 Plant Signaling & Behavior 87References1. Ariel FD, Manavella PA, Dezar CA, Chan RL. The true story of the HD-Zip family. T rendsPlant Sci 2007; 12:419-26.2. Lee YH, Chun JY. A new homeodomainleucine zipper gene from Arabidopsis thalianainduced by water stress and abscisic acid treatment. Plant Molec Biol 1998; 37:377-84. 3. T ron AE, Welchen E, Gonzalez DH. Engineering the loop region of a homeodomain-leucine zipper protein promotes efficient binding to a monomeric DNA binding site. Biochemistry 2004; 43:15845-51.4. Palena CM, Gonzalez DH, Chan RL. A monomer-dimer equilibrium modulates theinteraction of the sunflower homeodomain-leucine zipper protein HAHB-4 with DNA. Biochemistry 1999; 341:81-7.5. Palena CM, T ron AE, Bertoncini CW, Gonzalez DH, Chan RL. Positively charged residuesat the N-terminal arm of the homeodomain are required for efficient DNA binding by homeodomain-leucine zipper proteins. J Mol Biol 2001; 308:39-47.6. T ron AE, Bertoncini CW, Chan RL, Gonzalez DH. Redox regulation of plant homeodo-main transcription factors. J Biol Chem 2002; 277:34800-7.7. Mukherjee K, Burglin TR. MEKHLA, a novel domain with similarity to PAS domains, isfused to plant homeodomain-leucine zipper III proteins. Plant Physiol 2006; 140:1142-50.8. Schrick K, Nguyen D, Karlowski WM, Mayer KFX. START lipid/sterol-binding domainsare amplified in plants and are predominantly associated with homeodomain transcription factors. Genome Biol 2004; 41.9. De Caestecker MP , Yahata T, Wang D, Parks WT, Huang S, Hilli CS, Shioda T, Roberts AB,Lechleider RJ. The Smad 4 activation domain (SAD) is a proline-rich, p300-dependent transcriptional activation domain. J Biol Chem 2000; 3:2115-22.10. Sessa G, Steindler C, Morelli G, Ruberti I. The Arabidopsis ATHB-8, -9 and -14 genes aremembers of a small gene family coding for highly related HD-Zip proteins. Plant Mol Biol 1998; 38:609-22.11. Ohashi Y, Oka A, Pousada RR, Possenti M, Ruberti I, Morelli G, Aoyama T . Modulationof phospholipid signaling by GLABRA2 in root-hair pattern formation. Science 2003; 300:1427-30.12. Gago GM, Almoguera C, Jordano J, Gonzalez DH, Chan RL. Hahb-4, a homeobox-leucinezipper gene potentially involved in abscisic acid-dependent responses to water stress in sunflower. Plant Cell Environm 2002; 25:633-40.13. Wang Y, Henriksson E, Söderman E, Henriksson KN, Sundberg E, Engström P . TheArabidopsis homeobox gene, ATHB16, regulates leaf development and the sensitivity to photoperiod in Arabidopsis. Dev Biol 2003; 264:228-39.14. Olsson ASB, Peter Engstrom P , Soderman E. The homeobox genes ATHB12 and ATHB7encode potential regulators of growth in response to water deficit in Arabidopsis. Plant Mol Biol 2004; 55:663-77.15. Himmelbach A, Hoffmann T, Leube M, Hohener B, Grill E. Homeodoamin proteinATHB6 is a target of the protein phophatase ABI1 and regulates hormone responses in Arabidopsis. EMBO J 2002; 21:3029-38.16. Tahir M, Belmonte MF , Elhiti M, Flood H, Stasolla C. Identification and characterizationof PgHZ1, a novel homeodomain leucine-zipper gene isolated from white spruce (Picea glauca ) tissue. Plant Physiol Biochem 2008; 46:1031-9.17. Henriksson E, Olsson ASB, Johannesson H, Johansoon H, Hanson J, Engstrom P ,Soderman E. Homeodamin leucine zipper class I genes in Arabidopsis. Expression patterns and phylogentic relationships. Plant Physiol 2005; 139:509-18.18. Sessa G, Carabelli M, Sassi M, Ciolfi A, Possenti M, Mittempergher F , Becker J, Morelli G,Ruberti I. A dynamic balance between gene activation and repression regulates the shade avoidance response in Arabidopsis. Genes Dev 2005; 19:2811-5.19. Morelli G, Ruberti I. Light and shade in the photocontrol of Arabidopsis growth. T rendsPlant Sci 2002; 7:399-404.20. Sawa S, Ohgishi M, Goda H, Higuch K, Shimada Y, Yoshida S, Koshiba T . The HAT2 gene,a member of HD-Zip gene family, isolated as an auxin induciable gene by DNA microarray screening, effects auxin response in Arabidopsis. Plant J 2002; 32:1011-22.21. Rueda EC, Dezar CA, Gonzalez DH, Chan RL. Hahb , a sunflower homeodoamin-leucinezipper gene, is regulated by light quality and quantity, and promotes early flowering when expressed in Arabidopsis. Plant Cell Physiol 2005; 46:1954-63.22. Prigge MJ, Otsuga D, Alonso JM, Ecker JR, Drews GN, Clark SE. Class III homeodomain-leucine zipper gene family members have overlapping, antagonistic and distinct roles in Arabidopsis development. Plant Cell 2005; 17:61-76.23. Otsuga D, DeGuzman B, Prigge MJ, Drews GN, Clark SE. REVOLUTA regulates meristeminitiation at lateral position. Plant J 2001; 25:223-36.24. John L, Bowman JL, Floyd SK. Patterning and polarity in seed plant shoots. Annu RevPlant Biol 2008; 59:67-88.25. Emery JF , Floyd SK, Alvarez J, Eshed Y, Hawker NP , Izhaki A, Baum SF , Bowman JL.Radial patterning of Arabidopsis shoots by class III HD-Zip and KANADI genes. Curr Biol 2003; 13:1768-74.26. Baima S, Possenti M, Matteucci A, Wisman E, Altamura MM, Ruberti I, Morelli G. TheArabidopsis ATHB-8 HD-Zip protein acts as differentiation-promoting transcription factor of the vascular meristem. Plant Physiol 2001; 126:643-55.27. Abe M, Katsumata H, Komeda Y, Takahashi T. Regulation of shoot epidermal cell differen-tiation by a pair of homeodomain proteins in Arabidopsis. Development 2003; 130:635-43.was observed in plants with reduced ATHB-2 expression. A model explaining these phenotypes in relation to auxin distribution has been reviewed by Morelli and Ruberti.19 Tissue elongation was also induced by high expression of HAT-2, an auxin-inducible gene of the same class II.20 Response to dark and light conditions also involves HAHB-10, a sunflower gene with high similarity to ATHB-2. Ectopic expression of HAHB-10 in Arabidopsis produced a variety of phenotypic deviations, including dark cotyledons, planar leaves, reduced life cycle and accelerated flowering.21Members of HD-Zip class III play an important role during morphogenesis. Three proteins of this class, REV , PHB and PHV , control the pattern of apical formation during embryo develop-ment.22 Mutant analyses demonstrated the role of REV and PHB in regulating shoot apical meristem (SAM) maintenance and lateral organ initiation.23 Regulation of these morphogenic events might be caused by changes in auxin flow, since several members of HD-Zip class III have been implicated in events leading to changes of polar auxin transport.24 Several studies have elucidated the mode of action of REV , PHB and PHV , together with KANADI in control-ling abaxial-adaxial patterning of lateral organs.25 The abaxilation process and phloem differentiation are initiated by KANADI which also represses the expression of REV , PHB and PHV . This repres-sion is gradually released and expression of these three genes inhibits KANADI through feedback mechanisms and results in the adaxila-tion of the lateral organ and xylem formation.25 Another member of this class, ATHB-8 is also implicated in vascularization.26 Production of xylem is significantly increased in Arabidopsis plants overex-pressing this gene suggesting a possible role for ATHB-8 in inducing xylem element differentiation.26 This control however only occurs in the presence of specific cues since a reciprocal phenotype was not observed in lines with low ATHB-8 expression.The expression of several members of HD-Zip class IV is often restricted in the outer cells of plant organs where they regulate processes such as epidermal fate, trichome formation and antho-cyanin accumulation.23,27,28 The lack of epidermal cell identity in leaves of pdf2/atml1 double mutants argues for their involvement in epidermal identity acquisition. These genes might work in redundant fashion as denoted by the high degree of similarity. Proper trichome formation is also under the control of several members of this class. Genetic analyses revealed that hdg11/hdg12 double mutants produce highly branched trichomes. Further studies have revealed that HD-Zip IV members act redundantly with each other during devel-opmental events.29 Another gene of this class ANL2 is also involved in biosynthesis of anthocyanin in subepidermal tissues and cellular organization of primary root.28ConclusionsHD-Zip proteins are transcription factors unique to plants char-acterized by a homeodomain and a leucine zipper motif. Despite these structural similarities HD-Zip proteins participate in diverse and sometimes overlapping events ranging from stress responses to morphogenesis and development. Genetic analyses have revealed that their functions rely on the activation of downstream target genes the majority of which remain unknown. Elucidation of these downstream events will be key in understanding the role played by this important class of transcription factors.28. Kubo H, Peeters AJM, Aarts MGM, Pereira A, Koornneef M. ANTHOCYANINLESS2, ahomeobox gene affecting anthocyanin distribution and root development in Arabidopsis.Plant Cell 1999; 11:1217-26.29. Guan XY, Li QJ, Shan CM, Wang S, Mao YB, Wang LJ, Chen XY. The HD-Zip IV geneGaHOX1from cotton is a functional homologue of the Arabidopsis GLABRA2. PlantPhysiol 2008; 134:174-82.88Plant Signaling & Behavior2009; Vol. 4 Issue 2。

生物化学英语Introduction to BiochemistryBiochemistry is a fascinating interdisciplinary fieldthat combines biology and chemistry to study the chemical processes and molecules that occur within living organisms.It focuses on understanding the molecular mechanisms underlying biological processes and how they are regulated. In this document, we will provide an overview of important concepts and techniques in biochemistry.1. Structure and Function of BiomoleculesBiochemistry studies the structure and function of biomolecules, which include proteins, nucleic acids, carbohydrates, and lipids. Proteins are crucial for various cellular functions, such as enzyme catalysis, cell signaling, and structural support. Nucleic acids, including DNA and RNA, carry genetic information and are involved in protein synthesis. Carbohydrates are important energy sources, while lipids serve as components of cell membranes and energy storage molecules.2. Enzymes and MetabolismEnzymes are proteins that catalyze biochemical reactions, playing a vital role in metabolism. They lower the activation energy required for reactions to occur, thus speeding up the rate of chemical reactions within cells. Metabolism involves a series of interconnected biochemical reactions that convert nutrients into energy and building blocks for cellular processes. An understanding of enzyme kinetics and metabolic pathways is essential in biochemistry.3. Biochemical TechniquesVarious techniques are used in biochemistry to study biomolecules and their functions. These include spectroscopy, chromatography, electrophoresis, centrifugation, and molecular cloning. Spectroscopy allows the analysis of biomolecule structures by using light absorption, emission, or scattering. Chromatography separates mixtures into their individual components. Electrophoresis separates charged molecules based on their size and charge. Centrifugation separates particles based on their size and density. Molecular cloning allows for the replication and manipulation of DNA.4. Gene Expression and RegulationBiochemistry also encompasses the study of gene expression and regulation. Gene expression refers to the process by which information from a gene is used to produce a functional protein or RNA molecule. Regulation of gene expression ensures that the right genes are turned on or off at the appropriate times and in specific cell types. Understanding gene expression and regulation is crucial in understanding development, cell differentiation, and disease.5. Applications of BiochemistryBiochemistry has numerous applications in various fields, including medicine, agriculture, and biotechnology. In medicine, biochemistry is essential for understanding diseases at the molecular level and developing new drugs and therapies. In agriculture, biochemistry is used to improve crop yields and develop genetically modified organisms. Biotechnology relies heavily on biochemistry for geneticengineering, production of recombinant proteins, and designing new biofuels.ConclusionBiochemistry is a vast and dynamic field that plays a critical role in advancing our understanding of life processes and their applications. It provides a foundation for various other branches of biology and chemistry, contributing to fields such as molecular biology, genetics, and pharmacology. By studying the structure and function of biomolecules, enzymes, and metabolic pathways, biochemists continue to unravel the complexities of life.。

生长激素释放肽(ghrelin)促生长作用和应用前景来景辉;范红结【摘要】生长激素释放肽(ghrelin)是在大鼠和人胃内发现的,是一种生长激素促分泌素受体(growth hormone secretagogue receptor,GHSR)的内源性配体.ghrelin与位于垂体、下丘脑的GHSR结合后,具有促进生长激素释放、增加食欲、调节消化系统功能和能量代谢等作用.本文对ghrelin的结构、分布、生物学功能的近期研究成果及畜牧业上的应用前景进行综述,以期为相关添加剂的研究和开发提供依据.%Ghrelin, a peptide puried from rat and human stomachs, is an endogenous ligand for the growth hormone secretagogue receptor (GHSR). Ghrelin, after binding with GHSR in the hypothalamus and pituitary , not only promotes the GH releasing and increases appetite, but also adjusts the functions of digestive system and energy metabolism. This article mainly reviewed the recent developments on structure, distribution and biological functions of ghrelin as well as its potential applications on animal husbandry, which may lay the foundation for research and development of related additives.【期刊名称】《动物营养学报》【年(卷),期】2011(023)007【总页数】4页(P1085-1088)【关键词】生长激素释放肽;生长激素促分泌素受体;生物学功能【作者】来景辉;范红结【作者单位】宿州职业技术学院动物科学系,宿州234101;南京农业大学动物医学院,南京,210095【正文语种】中文【中图分类】S852.2生长激素释放肽(ghrelin)是生长激素促分泌素受体 (grow th hormone secretagogue receptor，GHSR)的内源性配体。

生化名词解释1.Isoelectrrc point (PI):AAs in solution at certaon PH are predominately in dipolary fom,fully ionized but without net charge due to-COO and-NH3+groups.2.Primary structure of protein:A linear connection of AAS along the protein chain,which is linked together by peptide.It is also calledamino sequence.3.Secondary structure of protein:A local spatial structure of a certain peptides segment,that is, the relatice position of backbone atoms ofthis peptide segment.4.Motift:When several local peptides of defined secondary structures are close enough space,they are able to forma Particularsular super-secondary structure.Forexample：Zincfinger,HLH(helix-loop-helix),HTH(helix-turn-helix),Leucine zipper.5.Pertiary structure:The spatial positions of all atoms of a protein, i..e,thethree-dimensional(3D) arrangement of all atoms.6.Auaternary structure:The spatial arrangement of multiple subunits of a protein.7.Domain:large polypeptides may be organized into structurally close but functionally independentunits.8.Denaturation:A process in which a protein loses its native conformation under the treatment of denaturants..(DEcreaes in solubility;incresse the visecosity;lose the biological activity;losecrystalizability;be susceptible to enzymatic digestion).9.Hybridization:TwoDNAs form different spacies are completely denatured by heating.When mixedand slowly plementary DNA strands of each species will associste and anneal to form normal duplexes.If the different dans have significance homology,the will teed to form partiarl duplexes or hybrids with cach other,this is called hybridization.10.Denaturation of DNA:The unfolding of the duplex strsnds into signle chains is referred to asdenaturation.11.Meltion temperature(TM):A260The temperature at which UV adsorption reaches the half of the maximum value as=lsomens that about 50％of the dsDNA is disassociated into the single-stranded DNA.12.Enzymes:A biomolecule. Either protion or nucleic acid, that catalyzes aspecific chemical reaction.They have extraordinary catalytic power and ahigh degree of spaecifity for their substrates.13.Active centers:Some functional groups are close enough in sasce to form a hydrophobic portion where substrates ar e catalyzed into products within the confines of a pocket on the enzyme.14.Isoenzyme:A group of enzymes that catalyze the same reaction but differ form each other in their structure,substrateaffinity, V max, and/of regulatory properties.15.Km:The substrate concentrates at which enzyme-catalyzed reaction proceeds at one-half itsmaximum velocity.16.Ribozymes:Ribonucleic acid(RNA) molecules with catalytic; RNA enzymes.17.Glycolysis:A molecule of glucose is degraded in a series of enzymatic reaction to yield two molecules of or lactate in cyto sol. glucoss(G)→lactic acid (lactic acid(lack of O2)18．Gluconeogenesis:The process of transformation of non-carbohydrates to glucose or glycogen.18.TCA:The reaction procedure is a cycle;form acetyl CoA+oxaloacetic acid→citric acid on,by a few times of dehydrogenesis and decarboxylation→oxaloacetic acid cycle;Also called citrate/Krebs cycle.19.Cori cycle:A metabolic process in which lactate,produced in tissues such as muscle,is transferred to liver where itbecomes a substrate in gluconeogenesis.(prevent acidosis;reduced lactate).20.AEerobic oxidation of glucose:The process of complete oxidation of glucose to CO2 and water with liberation of energy as The form of ATP.glucose(G)→H2O+CO2(O2)21.Biological oxidization:the process in which substance(Carbohydrate,lipid,AAs)are oxidized in living organism.22.Respiratory china(Electron transfer chain,ETC):A chain in the inner membrara of the mitochondria consists of redox carriers for transferring electronsform the substrate to molecular an oxygen ion,which combines with protons to form water.23.P/O ration:is the number of inorganic phosphates incorporates into ATP per oxyfen atom consumed.(Number of mol of ATP/2H)25.Hormone sensitive lipase (HSL):TG lipase is the rate-limiting enzyme in the TG degradation in adipose tissue.It is alsonamed HSL because it is regulated some hormones.26.Oxidative phosphorylation:The enzymatic phosphorylation of ADP to ADP coupled to clectron transfer from a substrate from a substrate to molecular oxygen.27.Substrate level phosphorylation:phosphorylation of ADP or some other nucleoside 5'-diphosphate coupled to the dehydrogenation of an organic substrate; independent of the electron transfer chain.28.Putrefaction of protein:some un-digested proteins and no absorbed are anaerobic by the bacteria in intestine. The products are toxic to body except few viamin and fatty acid.29.Essential fatty acids (EFA):Liinoleic, Linolenic and arechidonic acids are called essential fatty acids,because they cannot be synthesized by the body and must be obtained through diet.30.Fat mobilization:The triacyglycerol stored in the adipocytes are hydrolysized by lipsses,to produce free fatty acids(FFA) and glycerol, which are released to the blood, this process is called fat mobilization.31.Ketone bodies:water-soluble fuels normally exported by the liver but overproduced during fasting or in underated diabetes mellitus, including acetoactate, β-hydroxybutyrate,and acetone.32.Essential amino acids:acids that can not be synthesized by the body and must be obtained from the diet. 8 kinds of essential AAs: Val,Ile,LEU,Phe,Met,Trp,Thr,Lys.33.Union deamination:The α-amino group of most amino acids is transfereed to α-ketoglutarate toform a α-keto acid and glutamate by transaminase,Glutamate is then oxidatively deaminated to yied ammonia and α-ketoglutarate by glutamate dehydrogenase.34.One carbon unit:one carbon units(or groups) are one carbon-containing groups produced in catabolism of some amino acids. They are not free.-CH3,-CH2,-CH=,-CHO,-CH=CN.35.De noyo synthesis:The synthesis of nucleotides begins with their metabolic precursors: amino acids, ribose-5-phosphate,CO2,and one carbon units.36.Salvage pathways:The syntheses of nucleotide by recycie the free bases or nucleosides released from nucleic acid breakdown. 37.Replication:The separation of the two DNA strands,followed by synthesis of two new strands, each one complementary to a parental stand. So that eachnew formed double-helical ADNA contatins one parental strand and one daughter strand.38.Semi-conservative replication:The daughter strands on two parental strands are synthesized differently since the replication process obeys the principle that and DNA synthesis is in thedifferetlu since the replication process obeys the principle that the DNA synthesis is in the 5'-3'directuion.39.Leading strand:On the parental strand 3'-5'the daughter strand is synthesized continously.40.Okazaki fragments:The lagging strand synthesis processds discontinuously. These DNA fragments are called Okzaki fragments.41.Reverse transcription:a processin which ssRNA is used as the template to synthesize dsDNA by RNase. It Plays an important role in cancet-causing theory of viruses.42.Mutation:Mutation is a change of nucleic acids in genomic DNA of an organism,which could occur in the replication process s well as in other steps of life process.43.DNA repairing:a kind response made by the cells after DNA damage occurs, which may resume their natural structures and normal biological functions.44.Transcription:The synthesis of RNA molecules using DNA strands the templates so that the genetic information can be transferred from DNA to rna.45.Translation:the synthesis of protein molecules using mRNA as the template,in other words,to translate the nucleotide sequence of Mrna into the amino acid sequence of protein according to the genetic codon.46.Cis-acting elements:the DNA sequence that can affect the expression of its own gene composed of promoter, enhancer,and silencer.47.Trans-acting factors:the proteins that bind directly to cis-acting elements and regulate their activities.48.Exon:the coding sequence that appear on splice genes and primary transcription,and will be expressed to matured mRNA.49.Intron:the non-coding sequences that are transcripted into primary mRNAs, and will be cleaved out in the later splicing process.50.Activation of amino acid:in the first stage of protein synthesis, which takes place in the cytosol.The 20 differeent amino acids are etherified to their corresponding tRNA by aminoacyl-tRNA synthesis,each of which is specific for one amino acid and one or more corresponding Trna.51.Genetic codon:Three adjacent nucleotides in the 5'-3' direction on mRNA, which codes for an amino acid.52.S-D sequence:In Mrna of prokaryote, 8'-13 'nts prior to AUG, purine rich of 4-9 nts long,which is called ribosomal binding sequence.53.Prmoter:The DNA sequence that RNA-pol can bind to and initate transcription. Is is the key point for the transcription.54.Operon:Each transcription region, which is the basis of regulation of gene expression of prokaryotic systems,composed of structural genes, promoter, operator,and other regulatory sites.55.Gene:A DNA segment that encodes the all genetic information required to produce fanctional biological products.56.Genome:A complete set of genes of given species.57.Gene exptessin:briefly, it is gene transcription and translation. In detail, it is that production of proteins with biological activites according to the gene through transcription and translation.58.Housekeeping genes:The genes are essential and necessary for life, and therefore continuously expressed.such as those enzymes involved in TAC.59.Receptor:Receptor are specific membrane or intracellular proteins, which are able to recognize and bind to corresponding ligand molecules, become activated,and transducer signaling to next signaling molecules. They are usually glycoprotein or lipoprotein.60.Secondary messengers:small molecules synthesized with acell in response to an external signal are the second messenger,which are responsible for intracellular signal transduction. Ca,DG,Cer.IP3,cAMP,cGMP.。

二级结构英语Secondary Structure in EnglishThe secondary structure is an important concept in the field of protein structure analysis. It refers to the local folding patterns of the amino acid chain within a protein molecule. The primary structure of a protein, which is the linear sequence of amino acids, determines its secondary structure. In this article, we will explore the different types of secondary structures and their significance in protein function.The two most common types of secondary structures are alpha-helices and beta-sheets. Alpha-helices are right-handed coils formed by hydrogen bonds between the amino acid residues. They are characterized by a repeating pattern of 3.6 amino acid residues per turn and a rise of 1.5 angstroms per residue along the helical axis. Alpha-helices are often found in the transmembrane regions of membrane proteins and provide stability to the protein structure.On the other hand, beta-sheets are formed by hydrogen bonding between neighboring strands of amino acid residues. They can be either parallel or antiparallel, depending on the orientation of the strands. Beta-sheets are classified into two major types: beta-strands and beta-sheets. Beta-strands are the individual strands, while beta-sheets are formed by the alignment of multiple beta-strands. Beta-sheets are commonly found in the core regions of globular proteins and contribute to their structural stability.Apart from alpha-helices and beta-sheets, there are other secondary structures that play important roles in protein folding. One such structure is the beta-turn, also known as a reverse turn. Beta-turns are short segments of polypeptide chains that reverse their direction. They are characterized by the presence of a hydrogen bond between the carbonyl oxygen of one residue and the amide hydrogen of the residue three positions ahead. Beta-turns often connect two beta-strands in beta-sheets and are crucial for the folding of proteins.Another secondary structure is the random coil or loop region. As the name suggests, this region does not exhibit any regular folding pattern. Instead, it connects the secondary structure elements, allowing flexibility and movement within the protein molecule. Random coils are often found on the protein surface, where they play a role in protein-protein interactions and binding to ligands.The secondary structure of a protein is essential for its proper folding and function. It determines the overall shape and stability of the protein molecule. The folding of proteins into their native structures is driven by the interactions between the amino acid residues and the surrounding environment. These interactions include hydrogen bonds, electrostatic interactions, and hydrophobic interactions.In addition to their structural role, secondary structures also contribute to the functional properties of proteins. For example, alpha-helices can form transmembrane domains in membrane proteins, allowing them to anchor in the lipid bilayer. Beta-sheets can participate in protein-protein interactions, forming beta-sheets interactions or beta-sheets sandwiches. Beta-turns are often involved in protein-ligand binding, facilitating the recognition and binding of small molecules.In conclusion, the secondary structure of proteins is crucial for their folding, stability, and function. It encompasses various folding patterns, including alpha-helices, beta-sheets, beta-turns, and random coils. Each of these secondary structures plays a specific role in the overall structure and function of proteins. Understanding the secondary structure of proteins is essential for deciphering their biological functions and designing drugs that target specific protein structures.。

生化历来都不画重点的，但留学生老是过不了，于是就有了这个重点资料，和我们考的差不多，但是英语的，求高人翻译啊Brief Exercises of BiochemistryChapter 1 The structure and function of proteinExplain the following terms1. peptide bond2. Amino acid residues3. Primary structure of protein4. isoelectric point5. Secondary structure of protein6. Tertiary structure of protein7. Domain8. Protein denaturation9. Quaternary structure of proteinAnswer the following questions briefly1. What is physiological significance of hemoglobin oxygen dissociation curve as S-shaped?2. Please describe physiological functions of proteins.Discuss the following questions (Essay questions)1. Explain the relationship between the primary and spatial structure and the function of protein.Chapter 2 The structure and function of nucleic acidsExplain the following terms1. primary structure of nucleic acids2. DNA denaturation3. Tm4. DNA renaturation5. nucleic acid hybridizationAnswer the following questions briefly1. What is the structural characteristics of an eukaryocyte mature mRNA?2. What is the biological significance of Tm?Discuss the following questions (Essay questions)1. Please compare the two types of nucleic acids (DNA and RNA) in the chemical composition, molecular structure, cell distribution and biological functions.2. Please describe the structural characteristics of the B-DNA.3. Describe the molecular composition, structural features and functions of tRNA.Chapter 3 EnzymeExplain the following terms1. enzyme2. enzyme active center3. enzyme competitive inhibition4. Km5. isoenzyme6. zymogen activationAnswer the following questions briefly1. Explains with examples the competitive inhibition characteristic and the practical significance.2. What is the relationship between the enzyme cofactor and vitamine?3. What is the physiological significance of zymogen?4. What is isoenzyme? What is clinical significance of isoenzyme?5. How many kinds of essential group of enzyme are there? What is the role of each?Chapter 4 Metabolism of carbohydrateExplain the following terms1. glycolysis2. glycolytic pathway3. tricarboxylic acid cycle4. gluconeogenesis5. blood sugarAnswer the following questions briefly1. Describe briefly source and fate of blood sugar2. Describe briefly the physiological significance of gluconeogenesis3. Describe briefly the physiological significance of glycolysis4. Describe briefly the outline of TCA cycle5. Describe briefly the physiological significance of TCA cycle6. Describe briefly the physiological significance of pentose phosphate pathway7. Outline the reasons for the formation of lactic acid cycle and the physiological significance.8. Overview the important role of B vitamins in glucose metabolism.9. Why 6-phosphate glucose dehydrogenase activity will increase after uptake high-carbohydrate diet?Discuss the following questions (Essay questions)1. Explain how is lactate converted into glucose? (Write down the main reactions and key enzymes)2. Explain how is lactate converted into CO2, H2O and releases ATP? (Write down the main reactions and key enzymes)3. Overview the regulation molecular mechanism of adrenaline on the blood sugar level.4. Please explain why a slimmer has to reduce the intake of carbohydrates from the point of view of nutrients metabolism. (Write down the related pathways, cellular localization, main reactions and key enzyme)Chapter 5 Metabolism of lipidsExplain the following terms1. fat mobilization2. ketone body3. plasma lipoprotein4. apolipoprotein5. essential fatty acid6. blood lipidsAnswer the following questions briefly1. What is the function of bile acid at lipids digestion?2. What is the physiological significance of ketone body generation?3. What are materials of fatty acid synthesis?4. What is the physiological significance of cholesterol?5. What are the functions of apolipoprotein?Discuss the following questions (Essay questions)1. Describe the sources, chemical composition characteristics and main physiological functions of plasma lipoprotein.2. Explain how is the stearic acid converted into CO2, H2O and releases ATP?3. Please describe the oxidation catabolism process of glycerol generated from fat mobilization4. Explain how is the glycerol converted into glycogen?5. Describe the source and fate of acetyl-CoA?Chapter 6 Biological oxidationExplain the following terms1. biological oxidation2. respiratory chain3. oxidative phosphorylation4. substrate level phosphorylationDiscuss the following questions (Essay questions)1. Write down the sequence of two respiratory chainChapter 7 Metabolism of amino-acidExplain the following terms1. essential amino acid2. deamination of amino acid3. transamination of amino acid4. one carbon unit5. hyperammonemiaAnswer the following questions briefly1. What is the physiological significance of one carbon units?2. What is meaning of PAPS, GABA, SAM and FH4 each?3. Write down the deamination of amino acids in vivo.4. Outline the source and fate of blood ammonia.Discuss the following questions (Essay questions)1. How does a glutamate be oxidized to supply energy? What is the final product?2. What are functions of vitamins B in the metabolism of amino acids?3. Use the alanine as an example, try to explain the gluconeogenesis process of glucogenic amino acids.Chapter 8 Metabolism of nucleotideExplain the following terms1. de novo synthesis pathway of purine nucleotide2. nucleotide antimetaboliteAnswer the following questions briefly1. Outline the biological function of nucleotide.2. Outline the physiological significance of salvage synthesis of purine nucleotide.Discuss the following questions (Essay questions)1. Use the 6-mercaptopurine as an example, please explain the mechanism of antimetabolite.Chapter 10 Biosynthesis of DNAExplain the following terms1. semi-conservative replication2. reverse transcription3. replication4. excision repairing5. frame-shift mutationAnswer the following questions briefly1. Outline the classification and function of prokaryote DNA polymerase.2. Outline the classification and function of eukaryote DNA polymerase.3. Outline the factors causing DNA damage.4. Outline the repairing of DNA damage.5. Outline the central dogma.Discuss the following questions (Essay questions)1. Describe the materials involved in prokaryote DNA replication and their functions in that process.2. Describe the biological significance of mutation.Chapter 11 Biosynthesis of RNAExplain the following terms1. transcription2. posttranscriptional process3. hnRNA4. promoter5. ribozyme6. structure geneAnswer the following questions briefly1. Outline the eukaryote posttranscriptional process.2. Outline the products of three kinds of eukaryote RNA polymerases.Discuss the following questions (Essay questions)1. Describe the similarity and dissimilarity of replication and transcription.Chapter 12 Biosynthesis of proteinExplain the following terms1. translate2. polyribosomes3. genetic code4. degeneracy of codonAnswer the following questions briefly1. Describe briefly the RNAs involved in the protein synthesis and their functions in that process.2. Outline the main features of the genetic code.3. Describe briefly the dissimilarity of translation initiation complex formation of prokaryotes and eukaryotes.Discuss the following questions (Essay questions)1. Describe the materials involved in protein biosynthesis and their functions in that process.3. Please comparing the process of translation of prokaryotes and eukaryotes.Chapter 13 The regulation of gene expressionExplain the following terms1. gene expression2. cis-acting element3. trans-acting factor4. operon5. general transcription factor6. enhancerAnswer the following questions briefly1. What is biological significance of regulation of gene expression?2. Outline the function of each component of operon.3. What characteristics does eukaryotic genome structure have?Discuss the following questions (Essay questions)1. Explain the regulation mechanism of lactose operon.Chapter 14 Gene recombination and gene engineeringExplain the following terms1. restriction endonuclease2. genomic DNA3. vector4. cDNA. library5. genetic engineering6. DNA cloning7. homologous recombinationAnswer the following questions briefly1. What are the main selection criteria of gene vector?2. What is the significance of restriction endonuclease of bacteria themselves?3. At present, How many ways to get target genes?4. Outline the basic process of DNA cloning.Discuss the following questions (Essay questions)1. Why plasmid can be used as the vector of genetic engineering?2. Explain how to connect the foreign gene and the vector.3. What is α-complementary? Explain how to screening recombinant by it using an example.Chapter 15 Cellular signal transductionExplain the following terms1. signal transduction2. receptor3. ligand4. signal transduction pathway5. protein kinase6. second messenger7. G proteinAnswer the following questions briefly1. Describe briefly which protein kinases are regulated by intracellular second messenger.2. Outline the classification of receptor and its chemical signals.3. Describe briefly the basic mode of G protein-coupled receptor (seven transmembrane receptor)-mediated signal transduction.4. Describe briefly the signal transduction pathway of intracellular receptor of steroid hormone.Discuss the following questions (Essay questions)1. How does intracellular receptor play its function?2. Explain the process of the glycogen metabolism regulated by glucagon.3. Use fat mobilization as an example, explain the process of cAMP-protein kinase pathway. Chapter 16 Blood biochemistryExplain the following terms1. 2, 3-BPG shuntAnswer the following questions briefly1. Outline the function of plasma protein.Chapter 17 Liver biochemistrExplain the following terms1 biotransformation 2. primary bile acid 3. secondary bile acid4. bile pigment5. jaundiceAnswer the following questions briefly1. Describe briefly the physiological significance of biotransformation.2. Outline the main physiological functions of bile acids.3. Describe briefly production and blood transportation of bilirubin.Discuss the following questions (Essay questions)1. Describe the influence factor of biotransformation.2. Explain the dissimilarity of unconjugated and conjugated bilirubin.Chapter 18VitaminsExplain the following terms1. vitamin2. lipid-soluble vitamin3. water-soluble vitaminAnswer the following questions briefly1. Outline the biochemical function of vitamin E.2. Describe briefly the biochemical function of vitamin D and its deficiency disease.Discuss the following questions (Essay questions)1. Explain the relationship between the water-soluble vitamin and the coenzyme. Chapter 20 Oncogenes, tumor suppressor genes and growth factorExplain the following terms1. oncogene2. proto-oncogene3. tumor suppressor geneAnswer the following questions briefly1. Describe characteristics of proto-oncogene.2. Describe briefly wild-type p53 tumor suppressor gene mechanism.Chapter 21 The Principle and Application of Common Used Techniques in Molecular Biology Explain the following terms1. probe2. PCR3. Gene diagnosis4. gene therapyDiscuss the following questions (Essay questions)1. Describe the definition, type and application of the blotting technique.2. Describe the PCR reaction principle and the basic steps.。

2017年江西师范大学外国语学院357英语翻译基础考研真题及详解Ⅰ. 词语翻译：英汉术语、缩略语或专有名词互译（30分）（一）英译汉（15分）1. corpus-based system【答案】基于语料库的系统2. interlingual translation【答案】语际翻译3. interactive MT【答案】交互式机器翻译4. whispered interpreting【答案】耳语传译5. transmigration【答案】轮回；转生6. aesthetic equivalence【答案】审美对等7. community interpreting【答案】社区口译8. target-oriented【答案】目标导向9. hypotaxis【答案】形合10. governance in cyberspace【答案】网络空间治理11. cutting-edge technologies【答案】尖端技术12. the era of AI【答案】人工智能时代13. VR technology【答案】虚拟现实技术14. skopos theory【答案】翻译目的论15. translation and the dissemination of knowledge【答案】翻译与知识的传播（二）汉译英（15分）1. 功能对等【答案】functional equivalence2. 忠实通顺【答案】faithfulness and3. 语义翻译【答案】semantic translation4. 视译【答案】sight translation5. 逐字翻译【答案】word-for-word translation6. 不可译性【答案】untranslatability7. 信息经济示范区【答案】Information Economy Demonstration Zone8. 本地化【答案】localization9. 中国文化“走出去”【答案】“go global” strategy of Chinese culture10. 佛经翻译【答案】sutra translation11. 归化与异化【答案】domesticating translation and foreignizing translation12. 翻译与文化多样性【答案】translation and cultural diversity13. 计算机辅助翻译【答案】computer-assisted translation14. 非文学翻译【答案】non-literary translation15. 同声传译【答案】simultaneous interpretingⅡ. 语篇翻译：英汉段落互译（120分)（一）英译汉（60分）As information technology, specially the smartphone, rapidly develops, people are overwhelmed by all sorts of information. As a result, “smartphone addicts” can be seen everywhere…during meetings, lectures and gatherings; in the worst cases, such as when driving, they can cause disasters.Well, do people need to be inundated with so much information? We should remind ourselves that information doesn’t not equate to knowledge. Scattered information and fragmented reading not only cannot form anything useful in our minds but can rather actually interfere with our thinking, resulting in so-called “information overload”. Basically, information can be transformed into knowledge only when it is processed for a certain purpose featuring with a structure. In other words, when integrated into an individual system, knowledge functions as a part of a holistic effect.In terms of biological structure and functions the sensory organs of human beings are in fact no more developed than other highly evolved creatures, and yet humans can catch more of the essence of the world, mainly due to their abstract thinking capacity and their language systems. The secret lies in systematized structures.The core of a system is the structure which determines its nature and functions. Diamond and graphite(石墨), for example, are both made solely of carbons. However, their different arrangements of carbonaceous atoms result in the hardest and softest substance in the world. The same principle applies to our perceptual and knowledge systems, where the same amount of information may cause different effects. In a way, we may say “Knowledge is power”—But information is not.So-called “prediction” or “knowing the rest by analogy” is generated essentially by systematic analysis. Taking chemistry as an example, some gaps in the Periodic Table discovered by the Russian Chemist Mendeleyev predicted several new chemical elements; three of which were found by other chemists fifteen years later. Similarly, the theoretical physicist Diac revealed that there were no electronic “bubbles” in a vacuum dur ing his research into the nature of electrons, and then predicted that something called a “positron”(正子) might exist. In physics, many basic particles are found by way of repeated experiments based on symmetrical theory, thus bridging the gap between the subjective and objective worlds. In searching one of the greatest mysteries in modem astrophysics—dark matter—the same law applies.The transformation of “information” into “knowledge” requires ability. Information can be beneficial to our mental developmen t only if it has been effectively screened, categorized and stored. Blindly “receiving” information, on the other hand, will put us in a passive position where creativity can hardly be initiated.To be precise, a human’s intelligence therefore, doesn’t dep end on how much information he or she has been exposed to, rather, it is the ability to process information into personal constructive knowledge that counts.【参考译文】随着信息技术，特别是智能手机的飞速发展，人们被各种各样的信息淹没了。

Bioprocess 生物过程, 2015, 5(3), 30-37Published Online September 2015 in Hans. /journal/bp/10.12677/bp.2015.53005Research Progress on Molecular Structureand Biological Functions of HemocyaninZhenhuan Du, Jian Jing*Department of Biological Chemistry, Beijing Normal University, BeijingEmail: *jjing@Received: Sep. 5th, 2015; accepted: Sep. 23rd, 2015; published: Sep. 29th, 2015Copyright © 2015 by authors and Hans Publishers Inc.This work is licensed under the Creative Commons Attribution International License (CC BY)./licenses/by/4.0/AbstractHemocyanin is one of three main types of respiratory proteins and currently only occurs in mi-nority animal groups including arthropoda and molluscan species, respectively. Here we summa-rized the distribution and structural characteristics of hemocyanin superfamily members existing in the arthropoda and molluscan species, and the major biological features ever found were also introduced in detail. Commonly used techniques and methods during the investigation and re-search for the hemocyanin were listed and explained here. The above helps to understand the re-search status of hemocyanin and expand the practical application of it.KeywordsHemocyanin, Arthropoda, Molluscan, Molecular Structure, Biological Functions血蓝蛋白分子结构与生物学功能杜震环，井健*北京师范大学生物化学系，北京Email: *jjing@收稿日期：2015年9月5日；录用日期：2015年9月23日；发布日期：2015年9月29日*通讯作者。