BCMB2002 Lecture Notes - Lecture 2: Guanidine, Circular Dichroism, Protein Aggregation

• School: University of Sydney
• Department: Molecular Biology
• Course: BCMB2002
• Professor: bcmb2002

Document Summary

3d conformation native fold": has large no. of favourable interactions within the protein, there is a cost in conformational entropy of folding the protein into one specific native fold. H-bonds: release of water molecules from structured solvation layer around the molecule as protein, interaction of n-h and c=o of peptide bond leads to local regular structures (e. g. -helices. London dispersion (or induced dipole-induced dipole: one type of van der waals force (london & stronger dipole-dipole, medium-range weak attraction between all atom contributes significantly to stability in interior of the protein. Electrostatic interactions: long-range strong interactions between permanently charged groups, salt-bridges, esp. buried in the hydrophobic environment strongly stabilize the protein. Resonance causes peptide bonds: to be less reactive compared to esters, to be quite rigid & nearly planar, to exhibit large dipole moment in the favoured trans config. Polypeptide is made up of a series of planes linked at -c. The (cid:396)igid peptide pla(cid:374)e a(cid:374)d the pa(cid:396)tiall(cid:455) f(cid:396)ee (cid:396)otatio(cid:374)s.