Role of topological constraints in the all-or-none transition of a globular protein model: theory of the helix-coil transition in doubly crosslinked, coiled coils.
Employing a recently developed statistical mechanical theory, the alpha-helix-to-random-coil transition in two-chain, coiled coils is shown to possess many of the essential qualitative features of the equilibrium folding process in globular proteins. The role of short vs. long range interactions in stabilizing the native structure is examined. We demonstrate in doubly crosslinked coiled coils how, due to the role of loop entropy, an intrinsically continuous conformational transition evolves into one well approximated by an all-or-none transition. Thus the present work points out the crucial role played by loop entropy in the conformational transition in coiled coils in particular and perhaps in globular proteins in general.
D008956:Models, Chemical; D011487:Protein Conformation; D011506:Proteins
D011506:Proteins