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Lecture notes

Class notes 4BBY1013 (Biochemistry)

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Class lecture complete notes for biochemistry (4BBY1013) taken in the academic year ,

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November 28, 2023
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Lecture 05 - Protein Structure I


Learning 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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