BIOC 3560 Lecture Notes - Lecture 1: Dissociation Constant, Histidine, Coordinate Covalent Bond

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Properties of interest: size, molecular weight, hydrophobicity/ hydrophilicity, there is strong relation between a proteins structure and its function, protei(cid:374) stru(cid:272)tures are(cid:374)(cid:859)t flat charge. Reversible modification of protein function: proteins are dynamic molecules, function is influenced by interactions w other molecules. Interactions can be stable (on all the time and req. for protein to function) or transient (reversible, not on all the time) Prosthetic groups vs ligands: stable interactions: prosthetic groups are molecules that are permanently associated w a protein and is req. for its function, transient interactions: a ligand is a molecule that is bound reversibly by a protein. Binding sites and ligands: binding site: region of a protein surface that interacts with a ligand, complementary to ligand in, size, shape, charge, hydrophobicity/hydrophilicity. Interactions are highly specific: proteins can have 1 binding site. Induced fit: structural adaptation between protein and ligand. Conformation change can make binding site more complementary for optimal fit.

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