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Titolo:
Molecular dynamics of a 15-residue poly(L-alanine) in water: Helix formation and energetics
Autore:
Takano, M; Yamato, T; Higo, J; Suyama, A; Nagayama, K;
Indirizzi:
Univapanyo, Grad Sch Arts & Sci, Dept Life Sci, Meguro Ku, Tokyo 1538902, J Univ Tokyo Tokyo Japan 1538902 ept Life Sci, Meguro Ku, Tokyo 1538902, J Nagoyapaniv, Grad Sch Sci, Dept Phys, Chikusa Ku, Nagoya, Aichi 4648602, Ja Nagoya Univ Nagoya Aichi Japan 4648602 kusa Ku, Nagoya, Aichi 4648602, Ja Biomol Engn Res Inst, Suita, Osaka 5650874, Japan Biomol Engn Res Inst Suita Osaka Japan 5650874 uita, Osaka 5650874, Japan Natl Inst Physiol Sci, Okazaki, Aichi 4448585, Japan Natl Inst Physiol Sci Okazaki Aichi Japan 4448585 i, Aichi 4448585, Japan
Titolo Testata:
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
fascicolo: 4, volume: 121, anno: 1999,
pagine: 605 - 612
SICI:
0002-7863(19990203)121:4<605:MDOA1P>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALANINE-BASED PEPTIDES; SPECIAL-PURPOSE COMPUTER; ALPHA-HELIX; AMINO-ACIDS; FORMING TENDENCIES; FAST EVENTS; RELAXATION DYNAMICS; FOLDING DYNAMICS; COIL TRANSITIONS; SIMULATIONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Takano, M Univkyokyo, Grad Sch Arts & Sci, Dept Life Sci, Meguro Ku, 3-8-1Komaba, To Univ Tokyo 3-8-1 Komaba Tokyo Japan 1538902 u, 3-8-1 Komaba, To
Citazione:
M. Takano et al., "Molecular dynamics of a 15-residue poly(L-alanine) in water: Helix formation and energetics", J AM CHEM S, 121(4), 1999, pp. 605-612

Abstract

We present a molecular dynamics study of the alpha-helix formation in a system consisting of a 15-residue poly(L-alanine) and surrounding water molecules. By applying a relatively high temperature, we observed the alpha-helix formation several times during a 17-ns run, and reversible helix-coil transitions were also observed. The alpha-helix formations were usually initiated by the beta-tum structures. A crank-shaft-like motion of the peptide was included in the folding process. In the formed alpha-helical domains, substantial 3(10)-helix formations were found especially at the termini, as observed by the NMR study. The folding time scale at room temperature estimated from our simulation was found to lie in the range of 100ns, which is in accord with the time scale of the T-jump experiments. The total energy of the whole system was lower in the alpha-helix state than in the random-coil state by 20.4 +/- 4.8 kcal/mol, which is consistent with the experimental value obtained by calorimetry. This energy decrease in forming the alpha-helix was mainly caused by the Coulombic energy and the torsional energy.

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Documento generato il 20/09/20 alle ore 01:08:47