Helix/coil nucleation: a local response to global demands.

Abstract:

:A complete description of protein structure and function must include a proper treatment of mechanisms that lead to cooperativity. The helix/coil transition serves as a simple example of a cooperative folding process, commonly described by a nucleation-propagation mechanism. The prevalent view is that coil structure must first form a short segment of helix in a localized region despite paying a free energy cost (nucleation). Afterward, helical structure propagates outward from the nucleation site. Both processes entail enthalpy-entropy compensation that derives from the loss in conformational entropy on helix formation with concomitant gain in favorable interactions. Nucleation-propagation models inherently assume that cooperativity arises from a sequential series of local events. An alternative distance constraint model asserts there is a direct link between available degrees of freedom and cooperativity through the nonadditivity in conformational entropy. That is, helix nucleation is a concerted manifestation of rigidity propagating through atomic structure. The link between network rigidity and nonadditivity of conformational entropy is shown in this study by solving the distance constraint model using a simple global constraint counting approximation. Cooperativity arises from competition between excess and deficiency in available degrees of freedom in the coil and helix states respectively.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Vorov OK,Livesay DR,Jacobs DJ

doi

10.1016/j.bpj.2009.09.013

subject

Has Abstract

pub_date

2009-12-02 00:00:00

pages

3000-9

issue

11

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(09)01459-3

journal_volume

97

pub_type

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