Linked Life Data

8672715

Source:http://linkedlifedata.com/resource/pubmed/id/8672715

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-8-13
pubmed:abstractText
G. Makhatadze and P. Privalov [J. Mol. Biol., 226 (1995) 491] have recently measured the enthalpy of transfer of three proteins into urea and guanidinium chloride solutions as a function of concentration and temperature. The present paper applies the solvent-exchange model [J.A. Schellman, Biopolymers, (1994)] to the data and compares it with the binding model utilized in the original publication. Both calculations assume identical binding sites. It is found that the data may be fit tolerably well using either procedure, but that the parameters describing the binding vary considerably. Consideration of the transfer properties of amino acid moieties and small peptides leads to the conclusion that solvation sites are heterogeneous and that the quantities determined by both methods are statistical averages. The parameters describe an identical-site system that has (approximately) the same properties as the real heterogeneous system. The results have mainly heuristic and mechanistic value. One quantity determined with these simplified isotherms, sigma kj delta hj, is a property of the real system and can serve as a measure of a thermal binding capacity for a protein. The appendices contain a resume of the solution theory required for the exchange model of solvation as well as the development of a number of empirical equations for the thermodynamic properties of urea and guanidinium chloride solutions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
259-75
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The enthalpy of transfer of unfolded proteins into solutions of urea and guanidinium chloride.
pubmed:affiliation
Institute of Molecular Biology, University of Oregon, Eugene 97403, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.