Source:http://linkedlifedata.com/resource/pubmed/id/14664583
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
50
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pubmed:dateCreated |
2003-12-10
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pubmed:abstractText |
The thermal stability and folding kinetics of a 15-residue beta-hairpin (SESYINPDGTWTVTE) have been studied by using infrared (IR) spectroscopy coupled with laser-induced temperature-jump (T-jump) technique for rapid folding-unfolding initiation. An alternative method based on analyzing IR difference spectra was also introduced to obtain thermodynamic properties of beta-sheets, which complements the commonly used circular dichroism (CD) and fluorescence techniques. Equilibrium IR measurements indicate that the thermal unfolding of this beta-hairpin is fairly broad. However, it can be described by a two-state transition with a thermal melting temperature of approximately 29 degrees C. Time-resolved IR measurements following a T-jump, probed at 1634 cm(-1), indicate that the folding of this beta-hairpin follows first-order kinetics and is amazingly fast. At 300 K, the folding time is approximately 0.8 micros, which is only 2-3 times slower than that of alpha-helix formation. Additionally, the energetic barrier for folding is small (approximately 2 kcal mol(-1)). These results, in conjunction with results from other studies, support a view that the details of native contacts play a dominant role in the kinetics of beta-hairpin folding.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0002-7863
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
125
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15388-94
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:14664583-Amino Acid Sequence,
pubmed-meshheading:14664583-Kinetics,
pubmed-meshheading:14664583-Molecular Sequence Data,
pubmed-meshheading:14664583-Oligopeptides,
pubmed-meshheading:14664583-Protein Folding,
pubmed-meshheading:14664583-Protein Structure, Secondary,
pubmed-meshheading:14664583-Spectroscopy, Fourier Transform Infrared,
pubmed-meshheading:14664583-Thermodynamics
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pubmed:year |
2003
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pubmed:articleTitle |
Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.
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pubmed:affiliation |
Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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