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Titolo:
CONFORMATIONAL TRANSITION OF AN ALPHA-HELIX STUDIED BY MOLECULAR-DYNAMICS
Autore:
PLEISS J; JAHNIG F;
Indirizzi:
MAX PLANCK INST BIOL,CORRENSSTR 38 W-7400 TUBINGEN GERMANY
Titolo Testata:
European biophysics journal
fascicolo: 1, volume: 21, anno: 1992,
pagine: 63 - 70
SICI:
0175-7571(1992)21:1<63:CTOAAS>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEINS; SIMULATION; CONSTRAINTS; STATES; MOTION; MACROMOLECULES; MYOGLOBIN; DIFFUSION; NMR;
Keywords:
PROTEIN FOLDING; PROTEIN DYNAMICS; KRAMERS THEORY; RANDOM WALK; DIFFUSION;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
J. Pleiss e F. Jahnig, "CONFORMATIONAL TRANSITION OF AN ALPHA-HELIX STUDIED BY MOLECULAR-DYNAMICS", European biophysics journal, 21(1), 1992, pp. 63-70

Abstract

Molecular dynamics simulations were performed on a 20-residue polyalanine helix and a spontaneous transition from a kinked to a straight conformation was observed. The kinetics of the transition was analyzed within the framework of the Kramers model for chemical reactions and within a random walk model. The Kramers model which is based on diffusion along a one-dimensional reaction pathway and the crossing of an energy barrier was found to be inadequate. Instead, a random walk model based on diffusion in the high-dimensional phase space of the system wasfound to be compatible with the data. The high dimensionality of the phase space permits the system to circumvent high energy barriers and diffuse rapidly at about constant energy, but decelerates the reactionsince in the labyrinth of pathways the transition state is reached rarely.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 01:51:07