Linked Life Data

10679626

Source:http://linkedlifedata.com/resource/pubmed/id/10679626

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-4-4
pubmed:abstractText
The position of unfolding curves of oligomeric proteins depends on the protein concentration. The extent of this dependence is analyzed here in terms of the midpoint concentration, i.e., the denaturant concentration at which the fractions of folded and unfolded protein are equal. Reexamination of published data highlights that the midpoint concentration decreases as the protein concentration becomes lower, as expected. Moreover, there are differences between urea and guanidine hydrochloride, as well as discrepancies between the linear extrapolation model and the denaturant binding model. These discrepancies could be used to choose the denaturation model that best fits experimental data. The equations used can be applied to any oligomeric system to check the validity of the two-state assumption.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3525
pubmed:author
pubmed:copyrightInfo
Copyright 2000 John Wiley & Sons, Inc.
pubmed:issnType
Print
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
221-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
How the protein concentration affects unfolding curves of oligomers.
pubmed:affiliation
Dipartimento di Biochimica e Biofisica and CRISCEB, Seconda Università di Napoli, via Costantinopoli 16, 80138 Naples, Italy. ragone@unina2.it
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't