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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2004-3-3
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pubmed:databankReference |
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pubmed:abstractText |
An effort to combine theoretical analyses and protein engineering methods has been made to probe the folding mechanism of SH3 by using Energy Landscape Theory and a phi-value analysis. Particular emphasis was given to core residues and the effect of desolvation during the folding event by replacing the core valines with isosteric threonines. These mutations have the advantage of keeping the core structurally invariant while affecting core stability relative to the unfolded state. Although the valines that form the core appear spatially invariant, the folding kinetics of their threonine mutants varies, indicating their different extent of solvation in the transition-state ensemble. Theoretical studies predicted the distribution of folding kinetics of threonine mutants without previous knowledge of the measured rates. This initial success encourages further investigations of the molecular details behind these macroscopic phenomena and of the role of solvation in the folding mechanism.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-10430895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-10542091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-10611301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-10751944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-10801360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-11124040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-11326073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-11805324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-12446834,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-12684010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-1279434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-15012420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-1528885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-1569556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-1569557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-1569559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-1569560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-2314475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-2377205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-2739734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-3478708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-7509635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-9032067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-9348663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-9398297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-9465053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14978284-9571063
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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 |
Mar
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
101
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2834-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:14978284-Amino Acid Sequence,
pubmed-meshheading:14978284-Amino Acid Substitution,
pubmed-meshheading:14978284-Models, Biological,
pubmed-meshheading:14978284-Models, Molecular,
pubmed-meshheading:14978284-Mutagenesis, Site-Directed,
pubmed-meshheading:14978284-Protein Conformation,
pubmed-meshheading:14978284-Protein Denaturation,
pubmed-meshheading:14978284-Protein Folding,
pubmed-meshheading:14978284-Proteins,
pubmed-meshheading:14978284-Recombinant Proteins,
pubmed-meshheading:14978284-Solutions
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pubmed:year |
2004
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pubmed:articleTitle |
Solvation in protein folding analysis: combination of theoretical and experimental approaches.
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pubmed:affiliation |
European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117, Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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