Linked Life Data

9890889

Source:http://linkedlifedata.com/resource/pubmed/id/9890889

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-2-18
pubmed:abstractText
Annexins are ubiquitous cellular proteins of unknown primary function that bind to anionic phospholipid membranes in a calcium-dependent manner. Correlative studies involving X-ray crystallography and electron microscopy suggest that annexins undergo a structural change upon binding to supported lipid monolayer membranes. In this investigation, novel spectroscopic and analytical techniques have been applied to verify and characterize this change. Soluble annexin V was examined with ordinary transmission infrared spectroscopy, while membrane-bound annexin V was examined with both transmission and internal reflection infrared spectroscopy. Spectra were processed by linked analysis, whereby multiple spectra are fit simultaneously with component bands that are constrained to share common fitting parameters. This approach is shown to enhance the sensitivity and accuracy of the bandfitting procedure. Our results are consistent with the general mode of membrane binding inferred from electron microscopy studies, and they provide independent support for the conclusion that annexin V undergoes a conformational change upon binding to lipid monolayer membranes. Most likely, this change involves the formation of new beta structure in which interstrand hydrogen bonds orient parallel to the membrane surface.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
113-21
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Fourier transform infrared linked analysis of conformational changes in annexin V upon membrane binding.
pubmed:affiliation
Department of Pharmacology, Johnson Foundation for Molecular Biophysics, University of Pennsylvania, Philadelphia 19104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.