Linked Life Data

18217748

Source:http://linkedlifedata.com/resource/pubmed/id/18217748

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2008-2-14
pubmed:abstractText
We have investigated the orientation and conformation of protein molecules at the polystyrene (PS)/protein solution interface using sum frequency generation (SFG) vibrational spectroscopy, supplemented by attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). In this research, we studied fibrinogen as a model protein. SFG studies indicate that fibrinogen adopts a bent structure after adsorbing to the PS surface. A broad orientation distribution of fibrinogen coiled-coils at the interface has been quantified by combining SFG and ATR-FTIR measurements. Error analysis for such a deduced distribution was carried out. This research demonstrates that quantitative structural information such as orientational and conformational ordering of proteins at interfaces can be studied using SFG supplemented by other spectroscopic techniques.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1520-6106
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
112
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2281-90
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Quantifying the ordering of adsorbed proteins in situ.
pubmed:affiliation
Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't