[BIO 209] - Final Exam Guide - Comprehensive Notes for the exam (29 pages long!)
29 Nov 2016
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Document Summary
Amino acid arrangement and classification: alpha carbon- centrally located carbon with four branches that contain, r group, hydrogen atom, primary amino group, carboxyl group. Important in inducing 3d structures: peptide bonds- the covalent bond that links amino acids, amino/ carboxyl groups dictate the polarity in terms of direction of the polypeptide chain. **all peptides have an amino and carboxyl terminus** Higher order structure of proteins: primary- linear sequence of amino acids, secondary- spatial relations between amino acids that are not far apart, but are also not directly next to one another, alpha helix. Covalent bonds: disulfide bonds help stabilize protein structure. **intercellular proteins typically do not have disulfide bonds because they typically occur in proteins that are on the outside of a cell** Protein function: regulated by covalent modification, post translational controls- control mechanisms that occur after a protein is synthesized, kinetic properties of enzymes. **with an unsaturated reaction, there are no more substrate binding sites available.
