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Protein Biochemistry and enzymology $7.18
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Protein Biochemistry and enzymology
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  • Course
  • BI1014 - Biological Chemistry (BI1014)
  • Institution
  • Cardiff University (CF)

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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Document information

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

Subjects

  • proteins
  • enzymes
  • biochem
  • biochemistry
  • biomedical science
  • chromatography
  • equations
  • maths

Written for

  • Cardiff University (CF)
  • Unknown
  • BI1014 - Biological Chemistry (BI1014)
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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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