Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1996-9-12
pubmed:abstractText
The folding mechanism of a 125-bead heteropolymer model for proteins is investigated with Monte Carlo simulations on a cubic lattice. Sequences that do and do not fold in a reasonable time are compared. The overall folding behavior is found to be more complex than that of models for smaller proteins. Folding begins with a rapid collapse followed by a slow search through the semi-compact globule for a sequence-dependent stable core with about 30 out of 176 native contacts which serves as the transition state for folding to a near-native structure. Efficient search for the core is dependent on structural features of the native state. Sequences that fold have large amounts of stable, cooperative structure that is accessible through short-range initiation sites, such as those in anti-parallel sheets connected by turns. Before folding is completed, the system can encounter a second bottleneck, involving the condensation and rearrangement of surface residues. Overly stable local structure of the surface residues slows this stage of the folding process. The relation of the results from the 125-mer model studies to the folding of real proteins is discussed.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-1322172, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-1420144, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-1507227, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-1641003, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-1729690, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-2315699, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-2388698, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-270659, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-7563065, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-7613459, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-7618079, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-7648326, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-7680482, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-7710478, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-7773748, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-7893719, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-7937967, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8003983, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8060971, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8107095, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8180215, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8346235, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8513892, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8535237, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8592695, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8618859, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8710827, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-8846225, http://linkedlifedata.com/resource/pubmed/commentcorrection/8710875-9162942
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8356-61
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The folding mechanism of larger model proteins: role of native structure.
pubmed:affiliation
Committee on Higher Degrees in Biophysics, Department of Chemistry, Harvard University, Cambridge, MA 02138, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't