Literature DB >> 20366347

Random matrix approach to collective behavior and bulk universality in protein dynamics.

Raffaello Potestio1, Fabio Caccioli, Pierpaolo Vivo.   

Abstract

Covariance matrices of amino acid displacements, commonly used to characterize the large-scale movements of proteins, are investigated through the prism of random matrix theory. Bulk universality is detected in the local spacing statistics of noise-dressed eigenmodes, which is well described by a Brody distribution with parameter beta approximately = 0.8. This finding, supported by other consistent indicators, implies a novel quantitative criterion to single out the collective degrees of freedom of the protein from the majority of high-energy, localized vibrations.

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Year:  2009        PMID: 20366347     DOI: 10.1103/PhysRevLett.103.268101

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


  2 in total

1.  Constraints imposed by the membrane selectively guide the alternating access dynamics of the glutamate transporter GltPh.

Authors:  Timothy R Lezon; Ivet Bahar
Journal:  Biophys J       Date:  2012-03-20       Impact factor: 4.033

2.  ALADYN: a web server for aligning proteins by matching their large-scale motion.

Authors:  R Potestio; T Aleksiev; F Pontiggia; S Cozzini; C Micheletti
Journal:  Nucleic Acids Res       Date:  2010-05-05       Impact factor: 16.971

  2 in total

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