Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-7-9
pubmed:abstractText
The folding pathway and rate coefficients of the folding of a knotted protein are calculated for a potential energy function with minimal energetic frustration. A kinetic transition network is constructed using the discrete path sampling approach, and the resulting potential energy surface is visualized by constructing disconnectivity graphs. Owing to topological constraints, the low-lying portion of the landscape consists of three distinct regions, corresponding to the native knotted state and to configurations where either the N or C terminus is not yet folded into the knot. The fastest folding pathways from denatured states exhibit early formation of the N terminus portion of the knot and a rate-determining step where the C terminus is incorporated. The low-lying minima with the N terminus knotted and the C terminus free therefore constitute an off-pathway intermediate for this model. The insertion of both the N and C termini into the knot occurs late in the folding process, creating large energy barriers that are the rate limiting steps in the folding process. When compared to other protein folding proteins of a similar length, this system folds over six orders of magnitude more slowly.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-10972297, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-11114172, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-11601854, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-11972010, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-12773376, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-14988499, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-15102453, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-15268346, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-15531635, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-15549905, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-1594594, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-16008483, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-16043632, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-16392943, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-16469330, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-16608353, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-16710448, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-16787779, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-16821910, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-16978047, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-17169371, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-17368671, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-17517776, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-1762143, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-17747919, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-17911269, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-18052168, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-18554063, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-18588333, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-19015517, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-19211785, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-19421536, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-19485441, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-3477791, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-3478708, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-6347038, http://linkedlifedata.com/resource/pubmed/commentcorrection/20617197-8632455
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1553-7358
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
e1000835
pubmed:dateRevised
2011-4-1
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
The energy landscape, folding pathways and the kinetics of a knotted protein.
pubmed:affiliation
Department of Chemistry, Center for Theoretical Biological Physics, University of California San Diego, La Jolla, California, United States of America. mcprentiss@gmail.com
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural