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Lecture notes

Protein Biochemistry and enzymology
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Lecture notes from the BI1014 module Protein biochemistry and enzymology. Lecture notes written in 2023, some content missing due to strike action, however that will not be assessed this year.

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  • April 18, 2023
  • 6
  • 2022/2023
  • Lecture notes
  • Professor colin berry
  • All classes

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Enzymes

 Catalysts: Make reactions happen rapidly.
 Work under mild conditions.
 Specific for both reaction and substrate.
 Can be regulated.



 Substrate binds to enzyme (Rapidly reversible process).
 Reaction occurs and product(s) dissociate.

Low [S]: As [S] increases: High [S]:
At any instant only a small fraction of enzyme Most enzyme molecules
fraction of the enzyme molecules bound to have substrate bound.
molecules are substrate substrate increases. {SATURATION}
bound.

Michaelis-Menten equation

, Protein structure

Stabilisation of 3 ̊ Structure
 Van der Waals
 H-bonds

Disulphide Bonds
Covalent bonds
between two cysteine side-chains

-CH2-SH HS-CH2-
-CH2-S-S-CH2-

Ion pair bond (Salt Bridge) Ionisation




Domains
 Domain: globular unit formed from part of polypeptide.
o Domains often associated with a particular function EG yeast hexokinase.
o Large domain binds ATP Glucose binds between.

Quaternary Structure
Assembly of more than one polypeptide chain

Folding – Function
 Structure/Activity
 Necessary for drug design
 Necessary for protein engineering

Primary – Sequence of amino acids.
Secondary – Helices and sheets.
Tertiary – 3D structure – folded polypeptide.
Quaternary structure – Assembly of >1 folded polypeptide.

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