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Lecture about protein protein interaction
Example that we shall use is the interaction between an antibody and its antigen
Antibodies are a brilliant example of adaptation in biological systems.
The interaction between antigens and antibodies is exploited in our study of individual proteins.
Learning objectives:
By the end of your revision, you should understand the interactive forces that are responsible for stabilising the interactions that occur during biological processes. You should know why and how proteins are folded into simple secondary structures. Be familiar with the structure of antibodies and how the antigen binding site is generated. Understand the salient features that account for the interaction between lysozyme and the binding site of an antibody raised against it.
Background reading:
Introduction to Protein Structure
By Carl Branden John Tooze
Chapter 15
Standard Biochemistry text book
Eg. Biochemistry
By Reginald H. Garrett Charles M Grisham
Chapters 2 5
Interactive forces involved
Covalent bonds
Hold atoms together ( molecules
H, O, C and N are able to form covalent bonds by electron-pair sharing.
Lightest elements capable of forming these bonds.
H, O, C and N form the strongest covalent bonds
Two other covalent bond forming elements; phosphorus and sulphur
Weak chemical forces
Form intramolecular and intermolecular interactions between atoms:
Weak chemical Forces
Van der Waals forces
Hydrogen bonds Strength between
Ionic bonds 4 – 30 kJ/mol
Hydrophobic interactions
Not strong enough to bind free atoms together
But their cumulative number can impart stability by collective action is sufficient to impart stability to biological macromolecules
Because the interactions that occur during biomolecular recognition are sufficiently weak, they are readily reversible under physiological conditions.
Van der Waals Attractive Forces
Result of induced electrical interactions between closely approaching atoms or molecules as their neg
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