Linked Life Data

17655464

Source:http://linkedlifedata.com/resource/pubmed/id/17655464

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-7-27
pubmed:abstractText
Using the 28 residue betabetaalpha protein FSD-EY as a target system, we examine correction terms for the ECEPP/3 force field. We find an increased probability of formation of the native state at low temperatures resulting from a reduced propensity to form alpha helices and increased formation of beta sheets. Our analysis of the observed folding events suggests that the C-terminal helix of FSD-EY is much more stable than the N-terminal beta hairpin and forms first. The hydrophobic groups of the helix provide a template which promotes the formation of the beta hairpin that is never observed to form without the helix.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9606
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
035102
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Folding of a miniprotein with mixed fold.
pubmed:affiliation
John von Neumann Institut für Computing, Forschungszentrum Jülich, Jülich D-52425, Germany. s.mohanty@fz-juelich.de
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.