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Uspekhi Fizicheskikh Nauk, 2002, Volume 172, Number 11, Pages 1247–1269
DOI: https://doi.org/10.3367/UFNr.0172.200211b.1247
(Mi ufn2071)
 

This article is cited in 29 scientific papers (total in 29 papers)

REVIEWS OF TOPICAL PROBLEMS

Dynamical properties and energy landscape of simple globular proteins

Yu. F. Krupyanskii, V. I. Gol'danskiĭ

N. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow
References:
Abstract: Analysis of dynamic properties of a simple globular protein, myoglobin, has demonstrated that it possesses a hierarchically organized energy landscape. It shows two types of specific protein motions, besides vibrations: 1) individual motions of small atomic groups — transitions between conformational substates (CS) of the lower tier 2, and 2) cooperative motions of secondary structure elements ( α-helices) — transitions between CS of the upper tier 1. The profile of macromolecule dynamic properties is highly heterogeneous. Only vibrations occur near the active center. The number of CS grows towards the periphery where specific type 1 and 2 motions become predominant. Such a picture is consistent with the concept of a protein as 'a random copolymer slightly edited in the vicinity of the active center'.
Received: November 20, 2001
English version:
Physics–Uspekhi, 2002, Volume 45, Issue 11, Pages 1131–1151
DOI: https://doi.org/10.1070/PU2002v045n11ABEH001145
Bibliographic databases:
Document Type: Article
PACS: 87.10.+e, 87.15.By, 87.15.He, 87.80.-y
Language: Russian


Citation: Yu. F. Krupyanskii, V. I. Gol'danskiĭ, “Dynamical properties and energy landscape of simple globular proteins”, UFN, 172:11 (2002), 1247–1269; Phys. Usp., 45:11 (2002), 1131–1151
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  • This publication is cited in the following 29 articles:
    Citing articles in Google Scholar: Russian citations, English citations
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