Linked Life Data

17640069

Source:http://linkedlifedata.com/resource/pubmed/id/17640069

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-1-2
pubmed:abstractText
We have found that, contrary to naïve intuition, the degree of operational reversibility in the thermal denaturation of lipase from Thermomyces lanuginosa (an important industrial enzyme) in urea solutions is maximum when the protein is heated several degrees above the end of the temperature-induced denaturation transition. Upon cooling to room temperature, the protein seems to reach a state with enzymatic activity similar to that of the initial native state, but with higher denaturation temperature and radically different behavior in terms of susceptibility to irreversible denaturation. These results show that patterns of operational reversibility/irreversibility in protein denaturation may be more complex than the often-taken-for-granted, two-situation classification (reversible vs. irreversible). Furthermore, they are consistent with the possibility of existence of different native or native-like states separated by high kinetic barriers under native conditions and they suggest experimental procedures to reach and study such "alternative" native states.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1097-0134
pubmed:author
pubmed:copyrightInfo
(c) 2007 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19-24
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Beyond Lumry-Eyring: an unexpected pattern of operational reversibility/irreversibility in protein denaturation.
pubmed:affiliation
Facultad de Ciencias, Departamento de Quimica Fisica, 18071-Granada, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't