Lecture notes
Class notes 4BBY1013 (Biochemistry)
- Module
- (BIOCHEMISTRY)
- Institution
- Kings College London (KCL)
Class lecture complete notes for biochemistry (4BBY1013) taken in the academic year ,
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Lecture 05 - Protein Structure ILearning outcomes
Give examples of the functional role of proteins in living systems.
Explain that amino acids have an asymmetric carbon atom, and exhibit optical isomerism, existing in two conformations: D
and L.
Describe how amino acids may be classified on the basis of the properties of the side chains (R-groups), listing the major
categories of amino acid and giving examples.
Define ‘primary structure’.
Define the meaning of the terms: N-terminal, C-terminal, peptide bond, polypeptide.
Discuss properties of the peptide bond and their consequences for protein folding
Outline how the Ramachandran plot was used to predict features of protein structure
Describe the special properties of cysteine
Proteins perform many roles in the body
Lens of the eye
Hair
Antibodies
Muscle
Enzymes
Examples of protein performing many roles in the body
Each protein is unique and is determined by the information in the DNA sequence of the gene
, The building blocks of protein: amino acids
Proteins fold up spontaneously from linear chains of amino acid
The structure and characteristics of amino acids
Ionized form appears at physiological pH i.e., in the body
Amino acids are water soluble and electrically charged at physiological pH
Amino acids isomers: D and L
Asymmetric carbon atoms = enantiomers or optical isomers.
D and L refer to the geometry around the central carbon.
The L isomer is found in life.
Amino acid classification
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