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生物化学英文课件Biochemistry-chapter 3

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生物化学(英文版)biochemistry-chapter1英

生物化学(英文版)biochemistry-chapter1英

Secondary structure
Through biochemical research, people can understand the basic processes and mechanisms of organisms, explore the mechanisms of disease occurrence and development, and provide scientific basis for disease prevention, diagnosis, and treatment.
Biochemistry is an interdisciplinary field that aims to reveal the chemical essence behind life phenomena.
Definition of Biochemistry
Biochemistry helps to increase crop yield and improve quality in agriculture, and contributes to the development of nutritious, safe, and reliable new types of food in the food industry.
Large molecules in living organisms, such as proteins, nucleic acids, and polysaccharides, all have carbon as their core.
Carbon atoms can form complex network structures through covalent bonds, which endow biomolecules with high diversity and stability.
生物化学英文课件Biochemistry-chapter 3

生物化学英文课件Biochemistry-chapter 3

Requirement：1. Less cleave sites; 2. High specificity； 3. More production.
（1）Proteases cleavage：
1．Trypsin：C-terminal of Arg, Lys. High specificity
2．Chymotrypsin： C-terminal of Phe, Trp, Tyr.
1. Separation of amino acids by ion exchange chromatography
Amino Acid Separation
Unfortunately, amino acids are not colored as described in this overhead. Therefore, what methods would you use to first check if an amino acid is indeed present?
A-E-F-S-G-I-T-P-K
L-V-G-K
• Chymotrypsin Cleavage:
L-V-G-K-A-E-F S-G-I-T-P-K
• Edman degradation: L
• Correct sequence:
L-V-G-K-A-E-F-S-G-I-T-P-K
<2> Enzymatic hydrolysis：
7. Clostripain（Arg protease ）： c-terminal of Arg.
（2）Chemical cleavage：
1．CNBr： c-terminal of Met.
CNBr is useful because proteins usually have only few Met residues.
生物化学绪论 ppt课件

生物化学绪论 ppt课件

生物化学绪论
生物化学
一、生物化学的定义 生物化学(biochemistry) 是研究生物体内的化 学分子和化学反应的基础生命科学,从分子水平探讨 生命现象的本质，即生命的化学。 二、生物化学与分子生物学发展简史
二、生物化学与分子生物学发展简史
叙述生物化学阶段：18世纪中叶—19世纪末
动态生物化学阶段：20世纪初开始
1994年 生理学或医学奖 lfred G．Gilman（美国）Martin ROdbell（美国），发现 G蛋白及其在细 胞内信号转导中的作用 1993年 生理学或医学奖 Richard J．ROberts（美国）PhilliP A．SharP（美国），发现断裂基因化 学奖 Kary n．Mullis（美国），发明 PCR方法 Michael Smith（加拿大），建立 DNA合成用于定点诱变研究 1992年 生理学或医学奖 Edmond H．Fischer（美国）Edwin G．Krebs（美国），发现可逆蛋白质 磷酸化是一种生物调节机制 1989年 生理学或医学奖 Harold E．Varmus（美国）J．Michael Bishop（美国），发现反转录病毒 癌基因的细胞起源 化学奖 Sidney Altman（美国）Thorn R．Cech（美国），发现 RNA的催化性质 1988年 生理学或医学奖 James W．Black（英国）ertrude B．Elion（美国）Gong H．Hitchings（ 美国），发现“代谢”有关药物处理的重要原则
1964年 生理学或医学奖 Konard Bloch（美国）Feoder Lgnen（德国），发现胆固醇和脂肪酸代 谢的机制和调节 化学奖 Derothy Crowfoot Hodgkin（英国），用 X射线技术测定重要生化物质 的结构 1962年 生理学或医学奖 Francis H．C． Crick（英国）James D．Watson（美国）Maurice H． F． Wilkins（英国），发现核酸的分子结构（DNA双螺旋）及其对于活 性物质中信息转移的重要性 化学奖 Max F．Perutz（英国）JOhn C．Kendrew（英国），关于球状蛋白质 （血红蛋白、肌红蛋白）结构的研究 1959年 生理学或医学奖 Severo Ochoa（美国）Arthur KOrnbefg（美国），发现 RNA和 DNA生 物合成机制
biochemistry chapter3PPT课件

biochemistry chapter3PPT课件

▲the term proteome is derived from proteins expressed by the genome.
▲The genome tells us what is possible什么是可能的, the proteome tells us what is functionally present什么是(功能上)存在的
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• ▲e.g. which proteins interact to form a signal-transduction
pathway or an ion channel in a membrane
• ▲the proteome is not a fixed characteristic of the cell. Rather,
complex level of information content, the level of functional information, which encompasses the type, functions, and
interactions of proteins that yield a functional unit. 结构信息层面→功能信息层面(包括作为基本功能单位的蛋白的 类型,功能和相互作用)
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• How do AA sequences specify the
conformations of proteins?
• How do proteins bind specific substrates and
other molecules, mediate catalysis, and transduce energy and information?结合特异底 物和其它分子,催化反应,转换能量和信息.
生物化学英语版

生物化学英语版

生物化学英语版陈彻席亚明目录Chapter 1 Overview of Cell1.1 Structural Organization of Prokaryotic Cells1.2 Structural Organization of Eukaryotic CellsMembraneCytoskeletonThe NucleusThe Endoplasmic Reticulum and Golgi Apparatus MitochondriaLysosomes and PeroxisomesKey WordsChapter 2 Protein2.1 Amino AcidsGeneral Structures of Amino AcidsStructures of the 20 Common Amino AcidsSpectroscopic Properties of Amino AcidsThe Ninhydrin ReactionIonization of Amino Acids2.2 Structures of ProteinsPeptidePeptide BondsPrimary StructureSecondary StructureSupersecondary StructureTertiary StructureQuaternary StructureThe Classification of Proteins2.3 Structure-function Relationships of ProteinsPrimary Structure Determine the Conformation of Protein Protein Denaturation and RenaturationProtein StabilityCorrelation between Conformation and Function of Protein Protein Misfolding and Diseases2.4 Protein Purification TechniquesSalting OutDialysisGel Filtration ChromatographyIon Exchange ChromatographyAffinity ChromatographyElectrophoresisSDS Polyacrylamide Gel Electrophoresis （SDS-PAGE）Isoelectric FocusingTwo Dimensional ElectrophoresisUltracentrifugationKey WordsChapter 3 Enzymes3.1 The History of Enzymes3.2 Naming and Classification of EnzymesEC 1 OxidoreductasesEC 2 TransferasesEC 3 HydrolasesEC 4 LyasesEC 5 IsomerasesEC 6 Ligases3.3 Structural Components of EnzymesApoenzymes,Cofactors and HoloenzymesActive Center of EnzymesIsozymes3.4 The Properties of Enzymatic CatalysisEnzymes Greatly Accelerate the Rates of Chemical Reactions Specificity of EnzymesControllability of Enzyme Activity3.5 Mechanism of Enzymatic CatalysisTransition State and Activation EnergyLock and Key HypothesisInduced Fit HypothesisEnzyme-Substrate Interactions3.6 Enzyme KineticsSubstrate Concentration Affects the Rate of Reactions Michaelis-Menton KineticsThe Significance of KmMeasurement of Km and VmaxEnzyme Concentration Affects the Rate of Reactions Temperature Affects the Rate of ReactionspH Value Affects the Rate of ReactionsInhibition of Enzyme Catalyzed Reactions……Chapter 4 Coenzymes and VitaminsChapter 5 Nucleic AcidsChapter 6 DNA ReplicationChapter 7 RNA Synthesis-TranscriptionChapter 8 Protein Synthesis-TranslationChapter 9 Regulation of Gene ExpressionChapter 10 Carbohydrate MetabolismChapter 11 Electron Transport and Oxidative Phosphorylation Chapter 12 Lipid MetabolismChapter 13 Amino Acid MetabolismChapter 14 Nucleotides MetabolismChapter 15 Cell SignalingChapter 16 The Popular Techniques in Molecular Biology ReferenceIndex。

生物化学原理课件(英文)：Chapter32 Nucleotide Metabolism

生物化学原理课件(英文)：Chapter32 Nucleotide Metabolism


Why does UMP Cure Orotic Aciduria?
Carbamoyl Phosphate
X Orotate UMP Synthetase
Disease (-UMP)
– No UMP/excess orotate
Feedback Inhibition
☺Disease (+UMP)
Purines are synthesized on the Ribose ring
The metabolic origin of the nine atoms in the purine ring system
Many Steps Require an Activated Ribose Sugar (PRPP)
Catalyzes conversion of NDP to dNDP Highly regulated enzyme Regulates the level of cellular dNTPs Activated prior to DNA synthesis Controlled by feedback inhibition
The synthesis of AMP and GMP from IMP
Salvage Pathway for Purines
Hypoxanthine
or
+ PRPP = IMP or GMP + PPi
Guanine
(HGPRTase)
Adenine + PRPP = AMP + PPi
(APRTase)
de novo Pathway
Salvage Pathway
De novo Synthesis Committed step: This is the point of no return
生物化学课件Chapter 3 Amino acids and Peptides

生物化学课件Chapter 3 Amino acids and Peptides

• Later, enzyme digestion of proteins (much milder condition) helped to unveil which of these identified amino acids are actual building blocks of proteins.
DNA replication
Immune response (defending)
Light production (Luciferase)
O2 transport (Hemoglobin)
Support (keratin)
All proteins are constructed from the same set of 20 standard amino acids!
a
Common structure
1.
3.
The 20 amino acids are commonly categorized into five groups based on side chain features.
2. 4.
5.
Each amino acid possesses: 1. a common name 2. a three-letter abbreviation 3. an one-letter symbol
Biochemistry lecture 2 (Sept. 18, 2014)
Part I Structure and Catalysis
Chapter 3 Amino acids and Peptides
By Prof. Zengyi Chang (昌增益）
a-amino acid
Proteins are structurally and
生物化学-biochemistry ppt课件

生物化学-biochemistry ppt课件

5
Foundations of Modern Biochemistry
Goals of biochemistry Biochemistry seeks to describe the structure, organization, and functions of living matter in molecular terms.
12
Foundations of Modern Biochemistry
The idea of the gene, – a unit of hereditary information, – was first proposed in the mid-nineteenth century by Gregor Mendel.
(1) The structural chemistry of the components of living matter and the relationship of biological function to chemical structure.
(2) Metabolism – the totality of chemical reactions that occur in living matter.
(3) The chemistry of processes and substances that store and transmit biological information (Molecular Genetics).
8
Note
All living matters usually have the following properties :
living matter: 生物体; in molecular terms: 以分子的观点; at molecular levels: 从分子水平
unit3.biochemistry

unit3.biochemistry


过去完成时
1 着手研究之前就已经进行过的工作， 或已存在的状态。
一例16年前因患何杰金氏病接受过放 射治疗的22岁男患者发生放疗诱发的 甲状腺癌。
In a 22-year-old male, who had been irradiated 16 years previously for Hodgkin’s disease, a radiation-induced thyroid carcinoma developed.
2 介绍本文内容，常用的动词有： report报告, describe描述, present提出、 介绍, discuss讨论, review评述, emphasize, stress 强调、be是：
本文报导7例弥漫性血管内凝 血病。
The authors present 7 cases of disseminated散播 intravascular血 管内的 coagulation.
Text reading
1. have students read the text from the beginning to the end and then answer the questions.
2. explain some of the difficult points
论文及摘要的时态应用
练习
1 fill in the blanks the correct form of the verbs:
1) Resection of the rectum____ (perform) in 1395 patients.
was performed
2) During the past 15 years we have
【医学课件】生物化学(Biochemistry)

【医学课件】生物化学(Biochemistry)

2023【医学课件】生物化学(biochemistry)•生物化学简介•生物化学的基本概念•生物化学反应及代谢途径目录•生物氧化与能量代谢•遗传信息的传递与表达调控01生物化学简介生物化学是研究生物体中化学过程的科学，涉及生命体内各种化学物质、化学反应和能量转换等方面。

基本定义生物化学可分为分子生物学、细胞生物学、发育生物学等。

分类生物化学的定义与分类1生物化学的发展历程23生物学和化学的结合，诞生了生物化学这一学科。

19世纪末至20世纪初DNA双螺旋结构的发现、遗传密码的破译、酶的活性本质的研究等重大发现，极大地推动了生物化学的发展。

20世纪中叶随着分子生物学、细胞生物学等领域的发展，生物化学在医学领域的应用越来越广泛。

21世纪初生物化学与医学的关系01医学与生物化学密切相关，因为人体是一个复杂的生物化学系统，许多疾病的发生和发展都与生物化学过程有关。

02生物化学为医学提供了深入的理论基础和研究手段，如病因学、病理学、药物治疗等，对医学的发展起到了重要的推动作用。

03生物化学在医学中的应用包括基因诊断、药物治疗、免疫疗法等，为临床治疗提供了更多有效手段。

02生物化学的基本概念糖类多糖：多糖是由多个单糖分子通过聚合形成的，如淀粉、纤维素等。

二糖：二糖是由两个单糖分子通过脱水缩合形成的，如蔗糖、乳糖等。

单糖：单糖是构成多糖的基本单位，包括葡萄糖、果糖、核糖等。

总结词：糖类是生物体内重要的能量来源和物质构成，主要有单糖、二糖和多糖。

详细描述总结词：脂质是生物体内一类重要的分子，包括脂肪、类固醇、磷脂等。

详细描述脂肪：脂肪是细胞内重要的储能物质，由甘油和脂肪酸构成，具有保护和保温作用。

类固醇：类固醇是一类重要的生物活性物质，如胆固醇、性激素等。

磷脂：磷脂是细胞膜的主要成分之一，由甘油、脂肪酸和磷酸基团构成。

脂质01总结词：氨基酸是蛋白质的基本构成单位，蛋白质是一类复杂的有机高分子化合物。

氨基酸与蛋白质02详细描述03氨基酸：氨基酸是蛋白质的基本构成单位，由氨基、羧基、氢和R基组成。

【医学ppt课件】生物化学(Biochemistry)

【医学ppt课件】生物化学(Biochemistry)

2003年版； 3. Hames B et al., Instant notes in biochemistry(影印版)，
1999年版。
10
物质代谢变化与生理机能的关系——机能生物化学。
5
（三） 基因表达及其调控
转录
翻译
DNA
RNA
Pr
基因： 携带一定遗传信息的特定DNA片断以及相关的 调控序列；
（四） 专题生化
肝胆生化、水盐代谢和酸碱平衡等。
6
四. 生 物 化 学 与 医 药 学 的 关 系
与医学关系 2. 与药学关系 3. 与其他学科关系
【医学ppt课件】生物化学 (Biochemistry)
第一章 绪 论 （introduction)
2
一. 生物化学
主要是运用化学的理论和方法，从分子水平研究生 物体的化学组成及其在生命活动过程中化学变化规律 的一门学科，从而揭示生命现象的化学本质。
又称生命的化学(chemistry of life)。
3
二. 研 究 对 象
（主要针对组成生物体的六大营养素）： 糖、脂、蛋白质、核酸、水和无机盐等
4
三. 主要内容
（一）生物体的物质组成及其结构和功能
蛋白质、核酸和多糖 —— 生物大分子 / 生物信息分子 物质的组成、结构与化学性质等 —— 静态生物化学；
（二） 物质代谢及其代谢调节
物质在体内的代谢变化规律、能量代谢及其代谢调节是生 物化学的中心内容——动态生物化学；
7
五. 学 习 生 化 的 目 的
1. 了解生物体内物质的化学变化过程； 2. 从分子水平阐明疾病发生、发展的机制； 3. 更科学、有效地诊断与防治疾病，并帮助阐明中医
药的作用机理； 4. 指导新药的研制、提高对重大疾病的防治水平； 5. 为其他医药学基础课及临床医学打下扎实的基础。

Chapter 1 & 2 The Foundations of Biochemistry


The major types of biomolecules were revealed
The major types of biomolecules found in ALL types of living organism: proteins, carbohydrates, lipids and nucleic acids. Proteins, carbohydrates, and lipids were all discovered before the 19th century. Nucleic acids were the last of these to be isolated, in 1868, by Johann Friedrich Miescher, a Swiss, twenty-four years old.
Nobel prizes for Biochemical studies
1901-2006
A remarkable number of Nobel prizes have been won by biochemists
The aim of study:
To be able to read what is not written and to hear what is not said!
彻未书之道，悉言外之意
Lectured by 史 锋 shifeng@ 校园移动网：614263 Please feel free to contact me if you need！

The Nobel Prize in Physiology or Medicine 1988
Sir James W. Black
Gertrude B. Elion

Biochemistry 生物化学重点(英文)

Dear allFinally I finished the term and essay questions of biochemistry. I already choose the more important questions for all of you, which is attached in a word file.The exam will include choice questions (20 scores), term and essay questions (80 scores). “A leaf which falls from a tree goes wherever wind takes it. Be the wind to drive others, not the leaf to be driven by others.”“Success lies not in the result but in the effort. Being the best is NOT at all important; doing the best is all that matters!”“If you find your world as a sky and your friends as STARS, and if YOU don't find me among them, don’t worry! I've just been fallen to make your wish come true.”Best regard!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. Domain 8. Protein denaturation 9. 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 acids Explain 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 engineering Explain 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 biochemistryExplain 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 18 VitaminsExplain 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 factor Explain 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 UsedTechniques in Molecular BiologyExplain 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.。

生物化学课件Basic Biochemistry

long storage & form structures)
Macromolecule #1: Carbohydrates
Polysaccharide Examples:
Glycogen—glucose polymer stored for future energy needs. Found in liver, muscle and sperm, etc.
RNA: ribonucleic acid Genetic material, single stranded
ATP: adenosine triphosphate High energy compound
DNA
Nucleotide Structure
THE BIG PICTURE
Chemistry is essential for life…
Basic Biochemistry
What is Biochemistry?
Biochemistry is the study of the chemical interactions of living things.
Biochemists study the structures and physical properties of biological molecules.
Macromolecule #3: Proteins
The building blocks of proteins are AMINO ACIDS. There are only 20 types of Amino Acids.
There are millions of different proteins, and they are all built from different combinations of the 20 amino acids.

生物化学课件 protein


组氨酸 （His,H）
脯氨酸 （Pro,P）
芳香族氨基酸
苯丙氨酸 （Phe,F）
酪氨酸 （Tyr,Y）
色氨酸 （Trg,W）
非极性R基团氨基酸
不带电荷极性R基团氨基酸
带电荷R基团氨基酸
氨基酸的性质
(1)酸碱性质和等电点 (2)光学活性和光谱性质 (3)重要化学反应
•与2,4一二硝基氟苯(DNFB)的反应（sanger反应）:用 于蛋白质N-端测定. •与苯异硫氰酯（PITC）的反应（Edman反应）： 用于 蛋白N-端测定，蛋白质顺序测定仪设计原理的依据。
肽单位
肽键
肽平面
蛋白質的骨架 (Backbone)
N-端
C-端
两端 N-C-C-N-C-C-N-C-C-N-C-C
单位 N-C-C-N-C-C-N-C-C-N-C-C
肽键 N-C-C-N-C-C-N-C-C-N-C-C
-碳 N-C-C-N-C-C-N-C-C-N-C-C
R
R
R
R
Juang RH (2004) BCbasics
蛋白质的基本构件单位─氨基酸
一、常见的蛋白质氨基酸的结构通式 二、二十种常见的蛋白质氨基酸分类及结构 三、不常见的蛋白质氨基酸和非蛋白质氨基酸 四、氨基酸的性质 五、蛋白质的水解
L-α-氨基酸的结构通式
H │ H2N— C —COOH │ R
COOH
H2N C H 胺
R – - 氨基酸
三字母缩写 Gly Ala Val Leu Ile Pro Phe Tyr Trp Ser Thr Cys Met Asn Gln Asp Glu Lys Arg His
单字母符号 G A V L I P F Y W S T C M N Q D E K R H
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(2) Storage and transport of biochemical molecules (Hb, Mb)
(3) Physical cell support and shape (tubulin, actin, collagen)
(4) Mechanical movement (flagella, mitosis, muscles)
➢ (2) According to polymerization of protein molecules;
➢ Monomeric proteins ➢ Oligomeric proteins (multimeric proteins)
➢ (3) According to conjugation of protein molecules;
106 Da or more。 ➢ Usually insulin (5700 Da) or RNase (126000 Da)
was as the boundary of proteins and polypeptides. ➢ Mr of proteins ≈ Mr of amino acid ×110.
➢Mirror image pairs of amino acids are designated L (levo) and D (dextro)
➢Proteins are assembled from L-amino acids (few D-amino acids occur in nature)
Chapter 3 Amino Acids and the Primary
Structures of Proteins
3.1 Outline of Proteins 3.2 Structures of Amino Acids 3.3 Other Amino Acids and Amino
Acid Derivatives 3.4 Ionization of Amino Acids 3.5 Chemical reactions of AAs: 3.6 Peptide Bonds Link Amino Acids
Ball-and-stick model
Perspective
Fischer projections
Fischer projections - horizontal bonds from a
chiral center extend toward the viewer, vertical bonds extend away from the viewer
in Proteins
3.7 Protein Purification Techniques 3.8 Amino Acid Composition of Proteins 3.9 Determining the Sequence of Amino
Acid residues 3.10 Comparisons of the Primary
4. Configuration of amino acids.
Stereochemistry • Stereoisomers - compounds that have the
same molecular formula but differ in the arrangement of atoms in space • Enantiomers - nonsuperimposable mirror images • Chiral carbons - have four different groups attached
A.Aliphatic R groups: B.Aromatic R groups: C.Sulfur-containing R groups: D.Side chains with alcohol groups: E.Basic R groups: F.Acidic R groups and their amide
conformations of the peptide chain, such as a-helices and b-sheets ➢Tertiary structure - describes the shape of the fully folded polypeptide chain ➢Quaternary structure - arrangement of two or more polypeptide chains into multisubunit molecule
Proline has a nitrogen in the aliphatic ring system
• Proline (Pro, P) - has a three carbon side chain bonded to the a-amino nitrogen
• The heterocyclic pyrrolidine ring restricts the geometry of polypeptides = causes abrupt changes in the direction of the polypeptide chain
Mirror Images of Amino Acid
a
a
Mirror image of Stereoisomers
➢ The 19 chiral amino acids used in the assembly of proteins are all of the L configuration, although a few D-amino acids occur in nature.Why ?
(5) Decoding information in the cell (translation, regulation of gene expression)
(6) Hormones or hormone receptors (growth hormone, insulin receptor)
(7) Other specialized functions (antibodies, toxins etc)
3.2 Structures of Amino Acids
1. General structure of amino acids. More than 200 different AAs are
found in living organisms,including the 20 common (standard) amino acids.
• Proline (Pro, P) 3-carbon chain connects a-C and N = ring structure
Four aliphatic amino acid structures
Important in protein structure and folding since their R groups cluster away from water
COO-
Amino group
+ H3 N
a
Carboxylic group
H
R group
H = Glycine CH3 = Alanine
The R groups are different in 20 AAs.
Zwitterionic form of amino acids
• Under normal cellular conditions amino acids are zwitterions (dipolar ions): Amino group = -NH3+ (Protonated) Carboxyl group = -COO- (Ionized)
derivatives:
A. Aliphatic (hydrophobic) R Groups
• Glycine (Gly, G) - the a-carbon is not chiral since there are two H’s attached (R=H) = smallest and fits easiest into small nitches
5.Classification of the 20 common amino acids
(1).The three-letter and one-letter abbreviations.
(2). Classification of amino acids by chemical construction.
2. Classification of proteins:
(1) According to shape of prlar proteins
Usually water soluble, compact, roughly spherical Hydrophobic interior, hydrophilic surface globular proteins include enzymes, carrier and regulatory proteins
➢ Fibrous proteins
Provide mechanical support – not water soluble Often assembled into large cables or threads α-Keratins: major components of hair and nails Collagen: major component of tendons, skin, bones and teeth
Structures of Proteins Reveal Evolutionary Relationships
3.1 Outline of Proteins