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So my biochem course is really specific and doesn't cover metabolism at all. Will it be a major problem?
1. Principles of Biochemistry (2 lectures) The Foundations of Biochemistry Energy and principles of bioenergetics
2. Water (3 lectures) Non-covalent interactions
Properties of water
Acid/base properties, pH buffering capacity
3. Protein Structure and Stability (8 lectures)
Amino acids structures, nomenclature, chemistry.
Primary structure the peptide bond, sequence homology, and evolution, synthesis. Methods for protein purification and analysis.
Secondary structure α-helices, β-sheets, turns, Ramachandran plot, structure prediction. Tertiary structure, protein motifs & structure classification
Quarternary structure.
Protein folding and dynamics.
Methods for protein structure determination.
4. Protein Function (8 lectures) Chapters 5 and 6 Protein-ligand interactions. Oxygen-binding proteins.
Quantitative analysis of protein-ligand interactions.
Cooperativity, allostery.
Enzymes -- how they work.
Enzyme kinetics Michaelis-Menten equation, Lineweaver-Burke plots Enzyme inhibition mechanisms.
Examples of enzymatic reactions.
5. Carbohydrates and Glycobiology (2 lectures) 6. Nucleotides and Nucleic Acids (2 lectures)
7. Lipids and Membranes (2 lectures)
Chapter 7
Chapter 8
Chapters 10 and 11
Chapters 1 and 13 Chapter 2
Chapters 3 and 4
This as opposed to a more physiology related course focused on metabolism. What do you think?
1. Principles of Biochemistry (2 lectures) The Foundations of Biochemistry Energy and principles of bioenergetics
2. Water (3 lectures) Non-covalent interactions
Properties of water
Acid/base properties, pH buffering capacity
3. Protein Structure and Stability (8 lectures)
Amino acids structures, nomenclature, chemistry.
Primary structure the peptide bond, sequence homology, and evolution, synthesis. Methods for protein purification and analysis.
Secondary structure α-helices, β-sheets, turns, Ramachandran plot, structure prediction. Tertiary structure, protein motifs & structure classification
Quarternary structure.
Protein folding and dynamics.
Methods for protein structure determination.
4. Protein Function (8 lectures) Chapters 5 and 6 Protein-ligand interactions. Oxygen-binding proteins.
Quantitative analysis of protein-ligand interactions.
Cooperativity, allostery.
Enzymes -- how they work.
Enzyme kinetics Michaelis-Menten equation, Lineweaver-Burke plots Enzyme inhibition mechanisms.
Examples of enzymatic reactions.
5. Carbohydrates and Glycobiology (2 lectures) 6. Nucleotides and Nucleic Acids (2 lectures)
7. Lipids and Membranes (2 lectures)
Chapter 7
Chapter 8
Chapters 10 and 11
Chapters 1 and 13 Chapter 2
Chapters 3 and 4
This as opposed to a more physiology related course focused on metabolism. What do you think?
