Linked Life Data

11812146

Source:http://linkedlifedata.com/resource/pubmed/id/11812146

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-1-28
pubmed:abstractText
In the present work, we use structural information to characterize a set of disease-associated single amino acid polymorphisms exhaustively. The analysis of different properties, such as substitution matrix elements, secondary structure, accessibility, free energies of transfer from water to octanol, amino acid volume, etc., suggests that many disease-causing mutations are associated with extreme changes in the value of parameters relating to protein stability. Overall, our results indicate that, while knowledge of protein structure clearly helps in understanding these mutations, a finer understanding can come only from a quantitative knowledge of protein stability and of the protein environment in the cell. Interestingly, use of evolutionary information from multiple sequence alignments can be used to increase our knowledge of disease-associated mutations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2002 Academic Press.
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
315
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
771-86
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties.
pubmed:affiliation
Departament de Bioquímica i Biologia Molecular, Facultat de Química, Universitat de Barcelona, Spain.
pubmed:publicationType
Journal Article