Light-triggered beta-hairpin folding and unfolding

Schrader  TE; Schreier  WJ; Cordes  TKoller  FOBabitzki  GDenschlag  RRenner  CLoweneckt  MDong  SLMoroder  L

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Light-triggered beta-hairpin folding and unfolding

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A light-switchable peptide is transformed with ultrashort pulses from a beta-hairpin to an unfolded hydrophobic cluster and vice versa. The structural changes are monitored by mid-IR probing. Instantaneous normal mode analysis with a Hamiltonian combining density functional theory with molecular mechanics is used to interpret the absorption transients. Illumination of the beta-hairpin state triggers an unfolding reaction that visits several intermediates and reaches the unfolded state within a few nanoseconds. In this unfolding reaction to the equilibrium hydrophobic cluster conformation, the system does not meet significant barriers on the free-energy surface. The reverse folding process takes much longer because it occurs on the time scale of 30 mu s. The folded state has a defined structure, and its formation requires an extended search for the correct hydrogen-bond pattern of the beta-strand.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2007年第40期|15729-15734|共6页
作者
Schrader TE; Schreier WJ; Cordes TKoller FOBabitzki GDenschlag RRenner CLoweneckt MDong SLMoroder L;
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作者单位

Univ Munich, Lehrstuhl Biomol Opt, D-80538 Munich, Germany;

Univ Munich, Ctr Integrated Prot Sci, D-80538 Munich, Germany;

Max Planck Inst Biochem, D-82152 Martinsried, Germany;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
density functional theory calculation; peptide folding; TrpZip2; ultrafast infrared spectroscopy; MOLECULAR-DYNAMICS SIMULATIONS; VIBRATIONAL-SPECTRA; CONFORMATIONAL DYNAMICS; ATOMIC FLUCTUATIONS; FORCE-FIELD; PEPTIDE; SPECTROSCOPY; MODEL; PROTEINS; KINETICS;

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Light-triggered beta-hairpin folding and unfolding

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