The evolution dynamics of model proteins

Guido Tiana, Nikolay V. Dokholyan, Ricardo A. Broglia, Eugene I. Shakhnovich

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The use of evolution dynamics of model proteins for understanding the similarities between known proteins was discussed. The protein chains were described at a molecular, but simplified level. It was suggested that a number of evolutionary-related quantities, such as the distribution of sequence similarity for structurally similar proteins, are controlled by evolutionary kinetics and do not reflect an equilibrium state. The results for phylogeny show that a subset of the residues of each proteins evolve on a much larger time scale than other residues.

Original languageEnglish (US)
Pages (from-to)2381-2389
Number of pages9
JournalJournal of Chemical Physics
Volume121
Issue number5
DOIs
StatePublished - Aug 1 2004

Fingerprint

proteins
Proteins
set theory
Kinetics
kinetics

All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

Cite this

Tiana, G., Dokholyan, N. V., Broglia, R. A., & Shakhnovich, E. I. (2004). The evolution dynamics of model proteins. Journal of Chemical Physics, 121(5), 2381-2389. https://doi.org/10.1063/1.1768513
Tiana, Guido ; Dokholyan, Nikolay V. ; Broglia, Ricardo A. ; Shakhnovich, Eugene I. / The evolution dynamics of model proteins. In: Journal of Chemical Physics. 2004 ; Vol. 121, No. 5. pp. 2381-2389.
@article{a656596cf65a45e68ab7640f2d2be7d2,
title = "The evolution dynamics of model proteins",
abstract = "The use of evolution dynamics of model proteins for understanding the similarities between known proteins was discussed. The protein chains were described at a molecular, but simplified level. It was suggested that a number of evolutionary-related quantities, such as the distribution of sequence similarity for structurally similar proteins, are controlled by evolutionary kinetics and do not reflect an equilibrium state. The results for phylogeny show that a subset of the residues of each proteins evolve on a much larger time scale than other residues.",
author = "Guido Tiana and Dokholyan, {Nikolay V.} and Broglia, {Ricardo A.} and Shakhnovich, {Eugene I.}",
year = "2004",
month = "8",
day = "1",
doi = "10.1063/1.1768513",
language = "English (US)",
volume = "121",
pages = "2381--2389",
journal = "Journal of Chemical Physics",
issn = "0021-9606",
publisher = "American Institute of Physics Publising LLC",
number = "5",

}

Tiana, G, Dokholyan, NV, Broglia, RA & Shakhnovich, EI 2004, 'The evolution dynamics of model proteins', Journal of Chemical Physics, vol. 121, no. 5, pp. 2381-2389. https://doi.org/10.1063/1.1768513

The evolution dynamics of model proteins. / Tiana, Guido; Dokholyan, Nikolay V.; Broglia, Ricardo A.; Shakhnovich, Eugene I.

In: Journal of Chemical Physics, Vol. 121, No. 5, 01.08.2004, p. 2381-2389.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The evolution dynamics of model proteins

AU - Tiana, Guido

AU - Dokholyan, Nikolay V.

AU - Broglia, Ricardo A.

AU - Shakhnovich, Eugene I.

PY - 2004/8/1

Y1 - 2004/8/1

N2 - The use of evolution dynamics of model proteins for understanding the similarities between known proteins was discussed. The protein chains were described at a molecular, but simplified level. It was suggested that a number of evolutionary-related quantities, such as the distribution of sequence similarity for structurally similar proteins, are controlled by evolutionary kinetics and do not reflect an equilibrium state. The results for phylogeny show that a subset of the residues of each proteins evolve on a much larger time scale than other residues.

AB - The use of evolution dynamics of model proteins for understanding the similarities between known proteins was discussed. The protein chains were described at a molecular, but simplified level. It was suggested that a number of evolutionary-related quantities, such as the distribution of sequence similarity for structurally similar proteins, are controlled by evolutionary kinetics and do not reflect an equilibrium state. The results for phylogeny show that a subset of the residues of each proteins evolve on a much larger time scale than other residues.

UR - http://www.scopus.com/inward/record.url?scp=4043139258&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=4043139258&partnerID=8YFLogxK

U2 - 10.1063/1.1768513

DO - 10.1063/1.1768513

M3 - Article

C2 - 15260793

AN - SCOPUS:4043139258

VL - 121

SP - 2381

EP - 2389

JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

SN - 0021-9606

IS - 5

ER -