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)
BibTexBibNote ® (generic)BibNote ® (RIS) MedlineRefWorks
PT Journal Article
TI Dynamical properties and energy landscape of simple globular proteins
AU Krupyanskii Yu F
FAU Krupyanskii YF
AU Gol’danskii V I
FAU Gol’danskii VI
DP 10 Nov, 2002
TA Phys. Usp.
VI 45
IP 11
PG 1131-1151
RX 10.1070/PU2002v045n11ABEH001145
SO Phys. Usp. 2002 Nov 10;45(11):1131-1151

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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