Linked Life Data

2838982

Source:http://linkedlifedata.com/resource/pubmed/id/2838982

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
1988-8-11
pubmed:abstractText
ESR studies on spin-labeled amorphous RNase A as a function of varying concentrations of sorbed H2O and D2O will be presented. A relaxation analysis of saturation transfer (ST-)ESR spectra of 14N(1H) nitroxide spin-label molecules essentially fixed at amino acid residue His-105 will be given. A characteristic correlation has been observed between the microdynamic behavior--expressed by the rotational correlation times of the paramagnetic label--and the macroscopic thermodynamic entropy for the sorption process of H2O and D2O at RNase. This correlation is particularly pronounced at low water concentrations, vis., nH2O/nprotein less than or equal to 100. A significant difference in this concentration range exists between the two systems "RNase-H2O" and "RNase-D2O", which is manifested not only by the thermodynamic data but also by the microdynamic behavior extracted from the corresponding non-linear ESR absorption line shapes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0939-5075
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
285-93
pubmed:dateRevised
2009-11-4
pubmed:meshHeading
pubmed:articleTitle
Thermodynamic and magnetic resonance studies on the hydration of polymers: II. Protein-water interactions in powered ribonuclease.
pubmed:affiliation
Institut für Biophysik, Universität Witten/Herdecke, Witten-Annen, Bundesrepublik Deutschland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't