Class notes

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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Uploaded on April 18, 2023
Number of pages 6
Written in 2022/2023
Type Class notes
Professor(s) Professor colin berry
Contains All classes

proteins
enzymes
biochem
biochemistry
biomedical science
chromatography
equations
maths

Institution
Cardiff University (CF)
Education Unknown
Course
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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