Reviews of topical problems

Dynamical properties and energy landscape of simple globular proteins

Semenov Institute of Chemical Physics, Russian Academy of Sciences, ul. Kosygina, 4, Moscow, 119991, Russian Federation

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’.

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PACS: 87.10.+e, 87.15.By, 87.15.He, 87.80.−y (all)
DOI: 10.1070/PU2002v045n11ABEH001145
Citation: Krupyanskii Yu F, Gol’danskii V I "Dynamical properties and energy landscape of simple globular proteins" Phys. Usp. 45 1131–1151 (2002)
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RT Journal
T1 Dynamical properties and energy landscape of simple globular proteins
A1 Krupyanskii,Yu.F.
A1 Gol’danskii,V.I.
PB Physics-Uspekhi
PY 2002
FD 10 Nov, 2002
JF Physics-Uspekhi
JO Phys. Usp.
VO 45
IS 11
SP 1131-1151
DO 10.1070/PU2002v045n11ABEH001145

Оригинал: Крупянский Ю Ф, Гольданский В И «Динамические свойства и энергетичесий ландшафт простых глобулярных белков» УФН 172 1247–1269 (2002); DOI: 10.3367/UFNr.0172.200211b.1247

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