Linked Life Data

20873231

Source:http://linkedlifedata.com/resource/pubmed/id/20873231

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-9-28
pubmed:abstractText
The interaction of apomyoglobin and its mutant forms with phospholipid membranes was studied using tryptophan fluorescence and CD in the far UV-region. It is shown that a negatively charged phospholipid membrane can have a double effect on the structure of protein molecule upon their interaction: it denatures the native structure of the protein to its intermediate state similar to that in solution, acting as a moderately denaturing reagent. On the other hand, it can structure the unfolded protein to the same intermediate state stabilizing its structure. The kinetics of interaction between the protein and its mutant forms and the phospholipid membrane depends on the charge of the membrane surface. Here the rate of this interaction depends on the phospholipids vesicle concentration and the protein molecule stability increasing with a decrease of the latter. The importance of the obtained results for the folding of membrane proteins and the choice of the pathway for target delivery of protein drugs are discussed.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-8984
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
708-17
pubmed:meshHeading
pubmed:articleTitle
[Kinetics of interaction between apomyoglobin and phospholipid membrane].
pubmed:publicationType
Journal Article, English Abstract, Research Support, Non-U.S. Gov't