Role of Secondary Motifs in Fast Folding Polymers: A Dynamical Variational Principle
- 27 March 2000
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 84 (13) , 3009-3012
- https://doi.org/10.1103/physrevlett.84.3009
Abstract
A fascinating and open question challenging biochemistry, physics, and even geometry is the presence of highly regular motifs such as helices in the folded state of biopolymers and proteins. Stimulating explanations ranging from chemical propensity to simple geometrical reasoning have been invoked to rationalize the existence of such secondary structures. We formulate a dynamical variational principle for selection in conformation space based on the requirement that the backbone of the native state of biologically viable polymers be rapidly accessible from the denatured state. The variational principle is shown to result in the emergence of helical order in compact structures.
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This publication has 25 references indexed in Scilit:
- Protein Structures and Optimal Folding from a Geometrical Variational PrinciplePhysical Review Letters, 1999
- Steric Constraints in Model ProteinsPhysical Review Letters, 1998
- Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- Kinetic studies of β-sheet protein foldingCurrent Opinion in Structural Biology, 1998
- THEORY OF PROTEIN FOLDING: The Energy Landscape PerspectiveAnnual Review of Physical Chemistry, 1997
- From Levinthal to pathways to funnelsNature Structural & Molecular Biology, 1997
- Does Compactness Induce Secondary Structure in Proteins?Journal of Molecular Biology, 1994
- The Origins of Protein Secondary StructureJournal of Molecular Biology, 1994
- Properties and origins of protein secondary structurePhysical Review E, 1994
- On the Use of Classical Statistical Mechanics in the Treatment of Polymer Chain ConformationMacromolecules, 1976