Linked Life Data

10547279

Source:http://linkedlifedata.com/resource/pubmed/id/10547279

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-1-11
pubmed:abstractText
Folding of equine cytochrome c at a low protein concentration (26 microM) eliminated a slow kinetic phase (time constant three seconds) that was observed in the previous hydrogen exchange pulse-labeling experiments at pH 6.2 and 10 degrees C. It was demonstrated that this slow folding phase was caused by intermolecular aggregations. Because heterogeneous kinetics is a very general feature in the folding of proteins characterized by pulsed hydrogen exchange coupled with two-dimensional NMR, our experimental results suggest aggregations might also be responsible for the complex folding kinetics of other proteins. This is possible since these experiments were performed at relatively high protein concentrations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
293
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
991-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Intermolecular aggregations are responsible for the slow kinetics observed in the folding of cytochrome c at neutral pH.
pubmed:affiliation
Laboratory of Bioorganic Chemistry, National Institute Digestive and Kidney Diseases, NIH, Bethesda, MD 20892, USA.
pubmed:publicationType
Journal Article