Progressive stabilization of intermediate and transition states in protein folding reactions by introducing surface hydrophobic residues.

Abstract excerpt

It can be argued from the principle of solvent exclusion that the introduction of hydrophobic residues onto the surface of a protein will not destabilize the folded state because the nonpolar side chain will be at least as exposed in the unfolded state as it is when the protein chain is folded. A comparison of the folding pathway of wild type and 11 site-directed mutants of CD2.d1 shows this to be true. In fact,...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Disulfides
• Share to Guanidine
• Share to Immunoglobulins