Linked Life Data

1525171

Source:http://linkedlifedata.com/resource/pubmed/id/1525171

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1992-10-16
pubmed:abstractText
Using small-angle X-ray scattering and Fourier transform infrared spectroscopy, we have determined that the thermally denatured state of native ribonuclease A is on average a compact structure having residual secondary structure. Under strongly reducing conditions, the protein further unfolds into a looser structure with larger dimensions but still retains a comparable amount of secondary structure. The dimensions of the thermally and chemically denatured states of the reduced protein are different but both are more compact than is predicted for a random coil of the same length. These results demonstrate that thermal denaturation in ribonuclease A is not a simple two-state transition from a native to a completely disordered random coil state.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8329-35
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Denatured states of ribonuclease A have compact dimensions and residual secondary structure.
pubmed:affiliation
Life Sciences Division, Los Alamos National Laboratory, New Mexico 87545.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.