CAS BI 315 Lecture Notes - Lecture 3: Steric Effects, Reversible Reaction, Organic Compound
Document Summary
Amino acids and protein structure: side groups give polar, polar ionized, and nonpolar characteristics to amino acids, which is what gives properties to proteins. Primary structure: defines one protein versus another, the sequence of amino acids. Secondary structure: the folding and twisting due to amino acid properties. Tertiary structure: additional conformational changes by repulsive and attractive forces, 3-dimensional fixed structure (unless altered by a kinase or other enzyme) allows the protein to bind to a ligand, changing the conformation prevents binding to the ligand. Tight binding: all charges attract and the shapes match. High specificity: some proteins can have steric hindrance because of projections. Percent saturation: the percent of that protein type that is bound to a ligand. Allosteric changes: the alteration of a protein in a location not on the binding site that effects the protein"s ability to bind to a ligand. Diffusion: movement toward the random, even distribution of solutes.
