Linked Life Data

17301743

Source:http://linkedlifedata.com/resource/pubmed/id/17301743

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7129
pubmed:dateCreated
2007-2-15
pubmed:abstractText
The folding of small proteins has been assumed to be an all-or-none process that involves high cooperativity within the structure and substantial kinetic-energy barriers. Sadqi et al. claim that the small re-engineered protein Naf-BBL unfolds without significant cooperativity or kinetic hindrance, a conclusion that is based on calculation of a broad distribution of midpoint thermal-transition temperatures measured by the nuclear magnetic resonance (NMR) chemical shifts of 158 protons. We find that all of the unprocessed melting curves can be fitted to the same two-state global unfolding when uncertainties in the experimental data are taken into account. We conclude that the authors' melting data for Naf-BBL remain consistent with the all-or-none process.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1476-4687
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
445
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
E16-7; discussion E17-8
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Structural biology: analysis of protein-folding cooperativity.
pubmed:affiliation
Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, NIH, Building 37, Room 6114E, Bethesda, Maryland 20892, USA. yawen@helix.nih.gov
pubmed:publicationType
Journal Article, Comment