Linked Life Data

8073031

Source:http://linkedlifedata.com/resource/pubmed/id/8073031

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1994-9-28
pubmed:abstractText
An analysis of internal cavities in 121 protein chains has been undertaken to improve the characterization of their occurrence, morphology and role in protein tertiary structure, including an analysis of the optimal probe size for use in their detection. A number of basic cavity characteristics were elucidated. Cavities are non-artefactual and apparently independent of the method of structure determination, resolution and refinement of the data. Overall cavity volume increases with protein size and yet constitutes only a small fraction of the total protein volume but cavities are nearly always present in proteins > 100 residues in size. They are most commonly found in the protein core. 'Empty' and solvent-containing cavities have been compared and solvated cavities found to possess a more polar surface; the two classes are also seen to exhibit different amino acid type and secondary structural preferences. In general, residues that enclose cavities do not display any extra local mobility relative to their surrounding environments. Water-containing cavities do not impose volume restrictions upon their internal solvent beyond that of bulk solvent and permit good hydrogen bonding. These results should prove useful in protein modelling and design.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
613-26
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Intramolecular cavities in globular proteins.
pubmed:affiliation
European Molecular Biology Laboratory, Heidelberg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't