Dissipative dynamics and the statistics of energy states of a Hookean model for protein folding

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Küçük Resim

Tarih

2000-07

Dergi Başlığı

Dergi ISSN

Cilt Başlığı

Yayıncı

Kluwer Academic Publishers-Plenum Publishers

Erişim Hakkı

info:eu-repo/semantics/closedAccess

Araştırma projeleri

Organizasyon Birimleri

Dergi sayısı

Özet

A generic model of a random polypeptide chain, with discrete torsional degrees of freedom and Hookean spring connecting pails or hydrophobic residues, reproduces the energy probability distribution of real proteins over a very large range of energies. We show that this system with harmonic interactions, under dissipative dynamics driven by random noise, leads to a distribution of energy states obeying a modified one-dimensional Ornstein-Uhlenbeck process and giving rise Lo the so-called Wigner distribution. A tunably fine- or coarse-grained sampling of the energy landscape yields a family of distributions for the energies and energy spacings.

Açıklama

Anahtar Kelimeler

Protein folding, Dissipative dynamics, Charge-density waves, Universality, Relaxation, Spectrum, Behavior, Motions

Kaynak

Journal of Statistical Physics

WoS Q Değeri

Q2
Q2

Scopus Q Değeri

Q2

Cilt

100

Sayı

1-2

Künye

Tüzel, E. & Erzan, A. (2000). Dissipative dynamics and the statistics of energy states of a hookean model for protein folding. Journal of Statistical Physics, 100(1-2), 405-422. doi:10.1023/A:1018616417953