Dear learners,
Welcome to the biochemical world!
I am Professor Yang Rongwu from School of Life Sciences, Nanjing University. I have been teaching biochemistry for more than 25 years. I especially like Biochemistry and enjoy teaching Biochemistry.
First of all, I would like to thank you for taking this Structural Biochemistry MOOC!
Biochemistry is one of the fastest-growing and wide-ranging basic disciplines in the field of life sciences. It studies the life at the molecular level by using chemical, physical, and biological methods. Today, the theory and techniques of biochemistry have penetrated into every aspect of life sciences.
Biochemistry includes three parts: the fisrt one is Structural Biochemistry, which mainly studies the structure, function and properties of various biomolecules, the structure, properties and functions of various biomolecules, especially the three types of biomacromolecules, namely proteins, nucleic acids and enzymes; the second one is Metabolic Biochemistry, which mainly studies various chemical reactions in organisms;the third one is Molecular Biology, which mainly studies the storage, transmission, expression and regulation of genetic information.;
As the name suggests, this course is just focused on Structural Biochemistry, which can be regarded the most basic part of Biochemistry.
In this course, I used the vivid and strict scientific language, the elicitation method, a lot of interesting demonstrations to show you how wonderful, how useful and how important Structural Biochmeistry is. It firmly grasps the key point "structure determines function", combine theory with practice, and turn complicated and profound principles of biochemistry into interesting, popular, and useful knowledge, which greatly stimulates the learners' interest in learning and lays a solid foundation to study Metabolic Biochemistry, Molecular Biology, and other life sciences.
Finally, I wish you could study Biochemistry smoothly, happily and successfully! At the same time, I especially hope that you can put forward valuable opinions on this course, and then I can make improvements. Please email me at robertyang@nju.edu.cn or leave your message at the discussion section if you have any questions or opinions.
1.1 Amino acids
1.2 Proteinogenic AA & non-protenogenic AA
1.3 Hydrophobic & Hydrophilic AAs
1.4 Essential & Non-essential AAs
1.5 Abbreviations for 22 amino acids
1.6 AA Condensation reaction
1.7 Chirality of Amino Acids
1.8 Acid & base dissociation of amino acids and pI
1.9 Reaction with Ninhydrin
1.10 Reaction with DNFB
1.11 Reaction with PITC
1.12 Proteins
1.13 Primary Structure of Proteins
1.14 Peptide bonds
1.15 Secondary Structure of Proteins
1.16 The Alpha Helix
1.17 The Beta-Pleated Sheet
1.18 The Beta Turn
1.19 The Beta Bulge
1.20 Tertiary structure of Proteins
1.21 Hydrophobic interactions
1.22 Motif
1.23 Domain
1.24 Quaternary Structure of Proteins
1.25 Protein folding
1.26 Natively Unfolded Proteins
1.27 Anfinsen’s Experiment
1.28 Molecular Chaperone
1.29 Protein disulfide isomerase
1.30 Peptidylprolyl cis-trans isomerase
1.31 Prions
1.32 Proteome
1.33 Functions of Proteins
1.34 Moonlighting Proteins
1.35 Structure and function relationships of proteins
1.36 Alpha Keratin
1.37 Beta Keratin
1.38 Collagen
1.39 Myoglobin & Hemoglobin
1.40 Positive Cooperativity
1.41 Bohr Effect
1.42 Allosteric effect
1.44 HbS
1.44 HbF
Chapter 2 Structure and Function of Nucleic Acids
2.1 Bases
2.2 Keto-enol tautomerism
2.3 Nucleosides
2.4 Nucleotides
2.5 Nucleic Acids
2.6 Versatile RNAs
2.7 Primary Structure of Nucleic Acids
2.8 B-DNA
2.9 A-DNA
2.10 Z-DNA
2.11 Other forms of secondary structure of DNA
2.12 Secondary Structure of RNA
2.13 Tertiary Structure of DNA
2.14 Tertiary Structure of RNA
2.15 RNA-Protein Complex
2.16 Nucleosome
2.17 The RNA world
Chapter 3 Properties of Proteins and Nucleic Acids
3.1 UV absorption
3.2 Precipitation
3.3 Acid & base dissociation and pI
3.4 Denaturation
3.5 Renaturation
3.6 Tm
3.7 Hydrolysis
3.8 Protein coloring reaction
3.9 Electrophoresis
3.10 Chromatography
3.11 Dialysis and Ultrafiltration
Chapter 4 Structure and Function of Enzymes
4.1 Enzymes
4.2 Cofactors
4.3 Ribozymes
4.4 The Active Site
4.5 The Lock and Key Model
4.6 The Induced Fit Model
4.7 The Three-point Attachment Model
4.8 Enzyme Nomenclature
4.9 Enzyme Kinetics
4.10 The Mechaelis-Menten Equation
4.11 kcat and kcat/Km
4.12 The Double-Reciprocal Plot
4.13 Enzyme Inhibitors
4.14 Competitive Inhibitor
4.15 Non-competitive Inhibitor
4.16 Uncompetitive Inhibitor
4.17 Group Specific Reagent
4.18 Substrate Analogue
4.19 Suicide Inhibitor
4.20 Allosteric Enzymes
4.21 The Concerted Model
4.22 The Sequential Model
4.23 The Transition-State Stabilization Theory
4.24 Abzymes
4.25 Catalysis by Proximity and Orientation
4.26 General Acid-Base Catalysis
4.27 Electrostatic Catalysis
4.28 Metal Catalysis
4.29 Covalent Catalysis
4.30 Substrate Strain
4.31 Proteases
4.32 Regulation of Enzyme Activities
4.33 Isozymes
4.34 Allosteric Control
4.35 Regulation by Covalent Modification
4.36 Proteolytic Activation
4.37 Stimulation and Inhibition by Control Proteins
4.38 Vitamins
Chapter 5 Structure and Function of Carbohydrates and Lipids
5.1 Carbohydrates
5.2 Monosaccharides
5.3 Epimers
5.4 Anomer
5.5 Oligosaccharides
5.6 Polysaccharides
5.7 Glycoconjugates
5.8 Lipids
5.9 Free Fatty Acids
5.10 Fats
5.11 Trans Fats
5.12 Phospholipids
5.13 Cholesterol
5.14 Lipid Bilayers
Chapter 6 Structure and Function of Hormones
6.1 Hormones
6.2 Radio-immnoessay
6.3 Receptors
6.4 Second Messengers
6.5 G-proteins
6.6 Protein Kinases
6.7 Mechanism of Hormone Action by Intracellular Receptors
6.8 The PKA System
6.9 The PKC System
6.10 The PKG System
6.11 Nitric Oxide System
6.12 The RTK System
6.13 Visual Signal Transduction
6.14 Olfactory Signal Transduction
6.15 Termination of the Signal
