Linked Life Data

19545892

Source:http://linkedlifedata.com/resource/pubmed/id/19545892

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
2009-8-4
pubmed:abstractText
The effect of water-soluble phospholipid polymer conjugated to a protein on conformational change during heat-quenched stress was investigated in this study. Well-defined pyridine disulfide end-functional poly(2-methacryloyloxyethyl phosphorylcholine) (PMPC) was synthesized by well controlled atom transfer radical polymerization method. Synthesized PMPC was the site specifically conjugated to a protein, and the effect on conformational change during heat-quenched stress was estimated by circular dichroism and fluorescence study. As a result, a single phospholipid polymer chain conjugated to a protein give a great effect on conformational preservation in both secondary and tertiary structures even after the heat-quenched process. Moreover, even the conformational recovery which gave the completely reversible conformational preservation was observed in circular dichroism study. The resulting protein activity was also confirmed, and no significant decline was induced by heat-quenched stress.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1878-5905
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4859-67
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Conformational recovery and preservation of protein nature from heat-induced denaturation by water-soluble phospholipid polymer conjugation.
pubmed:affiliation
Department of Materials Engineering, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't