Linked Life Data

19580327

Source:http://linkedlifedata.com/resource/pubmed/id/19580327

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
2009-8-11
pubmed:abstractText
Understanding protein-solute interactions is one of the sizable challenges of protein chemistry; therefore, numerous experimental studies have attempted to explain the mechanism by which proteins unfold in aqueous urea solutions. On the basis of kinetic evidence at low urea concentrations, (1)H NMR spectroscopic analysis, and molecular orbital calculations, we propose a mechanistic model for the denaturation of RNase A in urea. Our results support a direct interaction between urea and protonated histidine as the initial step for protein inactivation followed by hydrogen bond formation with polar residues, and the breaking of hydrophobic collapse as the final steps for protein denaturation. With the proposed model, we can rationalize apparently conflicting results in the literature about the mechanism of protein denaturation with urea.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
18
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7608-13
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Molecular mechanism for the denaturation of proteins by urea.
pubmed:affiliation
Laboratorio de Genetica y Quimica Celular, Departamento de Biologia, Facultad de Ciencias, Universidad de Los Andes (ULA), Merida 5101, Venezuela.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't