BIOCHEM 523 Lecture Notes - Lecture 7: Protein Folding, Groel, Thermodynamics
3 Oct 2017
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Biochem423/523 - lecture 7 - tertiary and quaternary protein structure. G (folding) is typically -20 to -60 kj/mol. Hydrogen bonds (proton shared between two electronegative atoms, typically n. Van der waals interactions (induced dipole-induced dipole) It involves a decrease in randomness and a decrease in entropy when going from a. Salt bridges are electrostatic attractions between a positive charge and a negative random coil to a folded structure charge of a molecule at neutral ph. Weak induced dipole-induced dipole interactions between nonpolar groups can make. Water forms a cage-like structure called a clathrate around hydrophobic substances significant contributions to stabilizing proteins. The unfavorable conformational entropy change, which favors the unfolded state. The favorable enthalpy contribution arising from intramolecular noncovalent interactions. The favorable entropy change of the solvent arising from the burying of hydrophobic groups within the molecule. A more realistic energy landscape with local energy minima corresponding to stable intermediate states.
