Linked Life Data

15356870

Source:http://linkedlifedata.com/resource/pubmed/id/15356870

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-9-9
pubmed:abstractText
We describe here a new method for determining the conformational stability of antiparallel beta-sheets. Due to coupling between the transition dipoles, beta-sheet conformations typically exhibit a characteristic high-frequency amide I component centered at approximately 1680 cm(-1). Using one beta-sheet protein and two small beta-hairpins, we demonstrate that this high-frequency component, which is fairly narrow (approximately 8-10 cm(-1)), can be quantitatively resolved and used in thermal stability determination. Compared with the commonly used CD and fluorescence techniques, this ir method offers advantages. Since the area of this high-frequency component is only proportional to the folded population, it eliminates the need for a priori information of the folded and unfolded baselines encountered in other methods. Thus, it is applicable to a variety of beta-sheet systems.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3525
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
163-72
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Determining beta-sheet stability by Fourier transform infrared difference spectra.
pubmed:affiliation
Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural