Linked Life Data

20831285

Source:http://linkedlifedata.com/resource/pubmed/id/20831285

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
49
pubmed:dateCreated
2010-12-14
pubmed:abstractText
We report the application of pressure perturbation calorimetry (PPC) to study unfolded proteins. Using PPC we have measured the temperature dependence of the thermal expansion coefficient, ?(T), in the unfolded state of apocytochrome C and reduced BPTI. We have shown that ?(T) is a nonlinear function and decreases with increasing temperature. The decrease is most significant in the low (2-55 °C) temperature range. We have also tested an empirical additivity approach to predict ?(T) of unfolded state from the amino acid sequence using ?(T) values for individual amino acids. A comparison of the experimental and calculated functions shows a very good agreement, both in absolute values of ?(T) and in its temperature dependence. Such an agreement suggests the applicability of using empirical calculations to predict ?(T) of any unfolded protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1520-5207
pubmed:author
pubmed:issnType
Electronic
pubmed:day
16
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16166-70
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Pressure perturbation calorimetry of unfolded proteins.
pubmed:affiliation
Department of Biology and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
pubmed:publicationType
Journal Article