Literature DB >> 11018998

Role of secondary motifs in fast folding polymers: a dynamical variational principle.

A Maritan1, C Micheletti, J R Banavar.   

Abstract

A fascinating and open question challenging biochemistry, physics, and even geometry is the presence of highly regular motifs such as alpha 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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Year:  2000        PMID: 11018998     DOI: 10.1103/PhysRevLett.84.3009

Source DB:  PubMed          Journal:  Phys Rev Lett        ISSN: 0031-9007            Impact factor:   9.161


  8 in total

1.  A self-consistent knowledge-based approach to protein design.

Authors:  A Rossi; C Micheletti; F Seno; A Maritan
Journal:  Biophys J       Date:  2001-01       Impact factor: 4.033

2.  Role of native-state topology in the stabilization of intracellular antibodies.

Authors:  G Settanni; A Cattaneo; A Maritan
Journal:  Biophys J       Date:  2001-11       Impact factor: 4.033

3.  Universality classes in folding times of proteins.

Authors:  Marek Cieplak; Trinh Xuan Hoang
Journal:  Biophys J       Date:  2003-01       Impact factor: 4.033

4.  Folding pathways of prion and doppel.

Authors:  Giovanni Settanni; Trinh Xuan Hoang; Cristian Micheletti; Amos Maritan
Journal:  Biophys J       Date:  2002-12       Impact factor: 4.033

5.  Crucial stages of protein folding through a solvable model: predicting target sites for enzyme-inhibiting drugs.

Authors:  Cristian Micheletti; Fabio Cecconi; Alessandro Flammini; Amos Maritan
Journal:  Protein Sci       Date:  2002-08       Impact factor: 6.725

6.  The role of secondary structure in protein structure selection.

Authors:  Yong-Yun Ji; You-Quan Li
Journal:  Eur Phys J E Soft Matter       Date:  2010-05-25       Impact factor: 1.890

7.  Assessment of the quality of energy functions for protein folding by using a criterion derived with the help of the noisy go model.

Authors:  M Vendruscolo
Journal:  J Biol Phys       Date:  2001-06       Impact factor: 1.365

8.  Scaling of folding properties in go models of proteins.

Authors:  M Cieplak; T Xuan Hoang
Journal:  J Biol Phys       Date:  2000-12       Impact factor: 1.365

  8 in total

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