Linked Life Data

16870449

Source:http://linkedlifedata.com/resource/pubmed/id/16870449

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2006-8-28
pubmed:abstractText
The predominant equilibrium in proteins is not between native and unfolded states, it is between the native and multiple partially unfolded forms. Some of these partially unfolded forms can be energetically close to the native state and, therefore, have the potential to become appreciably populated. This could have an important role in protein function or misfolding diseases. The recent identification and characterization of the partially unfolded forms of apoflavodoxin furthers our understanding of their formation.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0968-0004
pubmed:author
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
494-6
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
The native-state ensemble of proteins provides clues for folding, misfolding and function.
pubmed:affiliation
Department of Biochemistry and BIFI, University of Zaragoza, Zaragoza 50009, Spain.
pubmed:publicationType
Journal Article, Comment, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural