Linked Life Data

16815056

Source:http://linkedlifedata.com/resource/pubmed/id/16815056

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-2-5
pubmed:abstractText
The results of protein pKa calculations are routinely being analysed to understand the pH-dependence of protein characteristics such as stability and catalysis. Systems of functionally important titratable groups are identified from protein from pKa calculations, but the rationalisation of the behaviour of such systems is inherently problematic due to a lack of theoretical tools and methods. I present a number of novel methods for analysing the results of protein pKa calculations which have been embedded in a graphical user interface (pKaTool). In the present paper I present novel methods for assessing the reliability of protein pKa calculations and for analysing the roles of individual residues in determining active site pKa values and the pH-dependence of protein stability. The methods presented are freely available to academic researchers at http://enzyme.ucd.ie/Science/pKa/pKaTool .
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1093-3263
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
691-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Analysing the pH-dependent properties of proteins using pKa calculations.
pubmed:affiliation
School of Biomolecular and Biomedical Science, Centre for Synthesis and Chemical Biology, UCD Conway Institute, University College Dublin, Belfield, Dublin 4, Ireland. Jens.Nielsen@ucd.ie
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't