BIOCHEM 4511 Study Guide - Final Guide: Biological Membrane, Reaction Rate, Membrane Lipids
4 Oct 2018
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Chapter 4: amino acids, peptide bond, protein structure, and protein. Understand tertiary structure and quaternary structure discussed in class including the types of bonds that hold them together. Forces that lead to specificity of tertiary protein structure: cross-links (disulfide bonds and metal centers), h-bonds, dipole-dipole interactions, ven der waals interactions, electrostatic interactions (salt bridges) Describe how proteins are folded/denatured and the properties of common denaturants. Chaotropes- small molecules commonly used to denature proteins; function by disrupting hydrophobic core of protein. Anfinsen demonstrated proteins can refold to a favored thermodynamic. Levinthal"s paradox is still in play: how do proteins fold in a reasonable. Protein folding: water as a solvent provides most of the driving force behind protein folding; proteins are amphipathic, they fold to maximize intramolecular hydrophobic interactions in aqueous solvent. Describe in detail a typical protein denaturation plot including the concept of cooperativity in protein folding or unfolding.
