Exposing the Nucleation Site in α-Helix Folding: A Joint Experimental and Simulation Study.

ABSTRACT: One of the fundamental events in protein folding is α-helix formation, which involves sequential development of a series of helical hydrogen bonds between the backbone C═O group of residues i and the -NH group of residues i + 4. While we now know a great deal about α-helix folding dynamics, a key question that remains to be answered is where the productive helical nucleation event occurs. Statistically, a helical nucleus (or the first helical hydrogen-bond) can form anywhere within the peptide sequence in question; however, the one that leads to productive folding may only form at a preferred location. This consideration is based on the fact that the α-helical structure is inherently asymmetric, due to the specific alignment of the helical hydrogen bonds. While this hypothesis is plausible

SUBMITTER: Acharyya A 

PROVIDER: S-EPMC6497059 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature