Linked Life Data

21609855

Source:http://linkedlifedata.com/resource/pubmed/id/21609855

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2011-5-25
pubmed:abstractText
The biophysical properties of proteins in the crowded intracellular environment are expected to differ from those for proteins in dilute solution. Crowding can be studied in vitro through addition of polymers at high concentrations. NMR-detected amide (1)H exchange is the only technique that provides equilibrium stability data for proteins on a per-residue basis under crowded conditions. We describe the theory behind amide (1)H exchange and provide a detailed description of the experiments used to quantify globular protein stability at the residue level under crowded conditions. We also discuss the detection of weak interactions between the test protein and the crowding molecules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1557-7988
pubmed:author
pubmed:copyrightInfo
Copyright © 2009 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
466
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-18
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Using NMR-detected backbone amide 1H exchange to assess macromolecular crowding effects on globular-protein stability.
pubmed:affiliation
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
pubmed:publicationType
Journal Article