10517642

Source:http://linkedlifedata.com/resource/pubmed/id/10517642

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0022702, umls-concept:C0033684, umls-concept:C0185026
pubmed:issue	6751
pubmed:dateCreated	1999-10-19
pubmed:abstractText	The detailed mechanism of protein folding is one of the major problems in structural biology. Its solution is of practical as well as fundamental interest because of its possible role in utilizing the many sequences becoming available from genomic analysis. Although the Levinthal paradox (namely, that a polypeptide chain can find its unique native state in spite of the astronomical number of configurations in the denatured state) has been resolved, the reasons for the differences in the folding behaviour of individual proteins remain to be elucidated. Here a Calpha-based three-helix-bundle-like protein model with a realistic thermodynamic phase diagram is used to calculate several hundred folding trajectories. By varying a single parameter, the difference between the strength of native and non-native contacts, folding is changed from a diffusion-collision mechanism to one that involves simultaneous collapse and partial secondary-structure formation, followed by reorganization to the native structure. Non-obligatory intermediates are important in the former, whereas there is an obligatory on-pathway intermediate in the latter. Our results provide a basis for understanding the range of folding behaviour that is observed in helical proteins.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0410462
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Staphylococcal Protein A
pubmed:status	MEDLINE
pubmed:month	Sep
pubmed:issn	0028-0836
pubmed:author	pubmed-author:KarplusMM, pubmed-author:ZhouYY
pubmed:issnType	Print
pubmed:day	23
pubmed:volume	401
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	400-3
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:10517642-Computer Simulation, pubmed-meshheading:10517642-Kinetics, pubmed-meshheading:10517642-Models, Molecular, pubmed-meshheading:10517642-Protein Folding, pubmed-meshheading:10517642-Staphylococcal Protein A, pubmed-meshheading:10517642-Thermodynamics
pubmed:year	1999
pubmed:articleTitle	Interpreting the folding kinetics of helical proteins.
pubmed:affiliation	Department of Chemistry & Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't