title: A physical basis for protein secondary structure.
abstract: A physical theory of protein secondary structure is proposed and tested by performing exceedingly simple Monte Carlo simulations. In essence, secondary structure propensities are predominantly a consequence of two competing local effects, one favoring hydrogen bond formation in helices and turns, the other opposing the attendant reduction in sidechain conformational entropy on helix and turn formation. These sequence specific biases are densely dispersed throughout the unfolded polypeptide chain, where they serve to preorganize the folding process and largely, but imperfectly, anticipate the native secondary structure.
authors.affiliation: Department of Biophysics, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
authors.forename: R
authors.initials: R
authors.lastname: Srinivasan
authors.forename: G D
authors.initials: GD
authors.lastname: Rose
mesh_terms: D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary