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Lecture 6

GENE 500 Lecture Notes - Lecture 6: Dissociation ConstantPremium

2 pages33 viewsFall 2018

Department
Genetics
Course Code
GENE 500
Professor
Lawrence Grossman
Lecture
6

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Lecture 6
Protein Design
Common principle in previously
listed types of function is ability to bind
to things (other proteins, ions, other
macromolecules....ligands)
Binding often involves
conformational changes
Binding is characterized by two
properties: affinity and specificity
Binding reflects molecular
complementarity
Antigen-antibody reaction is classic
example
Enzyme-substrate is second classic example
Proteins bind to one another, to other macromolecules, to small molecules, and to ions
The molecule to which a protein binds is called its ligand
In some cases, ligand binding causes a change in the shape of a protein
Such conformational changes are integral to the mechanism of action of many proteins
and are important in regulating protein activity
Specificity refers to the ability of a protein to bind one molecule or a very small group of
molecules in preference to all other molecules
Affinity refers to the tightness or strength of binding, usually expressed as the dissociation
constant (Kd).
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