Linked Life Data

16853544

Source:http://linkedlifedata.com/resource/pubmed/id/16853544

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
2006-7-20
pubmed:abstractText
The binding free energy of complex [Co(C(2)O(4))(3)](3-) to three peptides H-Lys-Gly-Lys-Gly-Lys-Gly-Lys-NH(2) (P-1), H-(Lys-Gly-Lys-Gly-Lys-Gly-Lys)(2)-NH(2) (P-2), H-(Lys-Gly-Lys-Gly-Lys-Gly-Lys)(3)-NH(2) (P-3) and to the monomers (amino acids) forming the peptides has been obtained using the kinetics of the electron-transfer reaction between [Ru(NH(3))(5)py](2+) and [Co(C(2)O(4))(3)](3-) as the probe. The polymerization of the monomers increases the negative free energy of binding and changes its character, noncooperative for the monomers and anticooperative for the peptides. This increase in the negative free energy represents a driving force for the polymerization process. The magnitude of the gain in negative free energy, as a consequence of the anticooperative character of the binding of the cobalt complex to the peptide, depends on the ratio of [complex]/[monomers].
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1520-6106
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
109
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19676-80
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Strength and character of peptide/anion interactions.
pubmed:affiliation
Centre de Biochemie Structurale CNRS UMR 5048 INSERM UMR 554, Université de Montpellier 1 29, route de Navacelles 34090 Montpellier Cedex, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't