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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
40
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pubmed:dateCreated |
2007-10-3
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pubmed:abstractText |
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 micros. 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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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-10430896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-12060746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-12621861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-12736378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-12946363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-14531687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-14741219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-15020773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-15041673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-15212506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-15452845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-15606241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-15606242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-15699340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-15740129,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-16172406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-16305213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-16494351,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-16837192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-16853169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-3541539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-9367160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17893334-9933907
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
pubmed-author:BabitzkiGalinaG,
pubmed-author:CordesThorbenT,
pubmed-author:DenschlagRobertR,
pubmed-author:DongShou-LiangSL,
pubmed-author:KollerFlorian OFO,
pubmed-author:LöweneckMarkusM,
pubmed-author:MoroderLuisL,
pubmed-author:RennerChristianC,
pubmed-author:SchraderTobias ETE,
pubmed-author:SchreierWolfgang JWJ,
pubmed-author:VaccoP JPJ,
pubmed-author:ZinthWolfgangW
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
104
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15729-34
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17893334-Amides,
pubmed-meshheading:17893334-Carbon,
pubmed-meshheading:17893334-Light,
pubmed-meshheading:17893334-Magnetic Resonance Spectroscopy,
pubmed-meshheading:17893334-Models, Molecular,
pubmed-meshheading:17893334-Oxygen,
pubmed-meshheading:17893334-Peptides,
pubmed-meshheading:17893334-Protein Conformation,
pubmed-meshheading:17893334-Protein Denaturation,
pubmed-meshheading:17893334-Protein Folding,
pubmed-meshheading:17893334-Protein Structure, Secondary,
pubmed-meshheading:17893334-Spectrophotometry, Infrared
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pubmed:year |
2007
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pubmed:articleTitle |
Light-triggered beta-hairpin folding and unfolding.
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pubmed:affiliation |
Munich Center for Integrated Protein Science, Ludwig-Maximilians-Universität München, Oettingenstrasse 67, 80538 Munich, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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