Linked Life Data

12379110

Source:http://linkedlifedata.com/resource/pubmed/id/12379110

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
2002-10-15
pubmed:abstractText
Unfolded apomyoglobin in 8 M urea at pH 2.3 displays distinct regions with different backbone mobility, as monitored by NMR relaxation. These variations in backbone mobility can be correlated with intrinsic properties of the amino acids in the sequence. Clusters of small amino acids such as glycine and alanine show increased backbone mobility compared to the average. In contrast, local hydrophobic interactions that persist in urea denaturant cause some restriction of backbone motions on a picosecond to nanosecond time scale. The model derived from the behavior of apoMb in urea depends only on the most fundamental properties of the local amino acid sequence, and thus provides a feasible paradigm for the initiation of folding.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12681-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Molecular hinges in protein folding: the urea-denatured state of apomyoglobin.
pubmed:affiliation
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't