Linked Life Data

12625829

Source:http://linkedlifedata.com/resource/pubmed/id/12625829

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-3-10
pubmed:abstractText
Temperature and Guanidine hydrochloride induced unfolding transitions of papain at pH 2.0 are biphasic implying independent and sequential unfolding of its two domains. To determine the order of unfolding, the active site located in the interface of the domains was labeled with an environment specific fluorescent probe (1,8-IAEDANS). Unfolding of this complex relative to the free protein followed by intrinsic and extrinsic fluorescence measurements suggests that the N domain unfolds initially in the sequential unfolding of domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0929-8665
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
83-90
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
N-terminal domain unfolds first in the sequential unfolding of papain.
pubmed:affiliation
Department of Biochemistry, Institute of Medical Sciences, Banaras Hindu University, Varanasi 221005, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't