Linked Life Data

3210232

Source:http://linkedlifedata.com/resource/pubmed/id/3210232

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-2-14
pubmed:abstractText
Available crystallographic data for homologous immunoglobulin constant domains were correlated with measured association constants for these domains. High correlation was found between the association constant and both the buried surface area (number of interdomain contacts) and the number of salt bridges formed in the interaction, whereas no correlation with the number of hydrogen bonds between domains was evident. The total free energy of binding, as determined from the association constant, was related to the number of contacts, hydrogen bonds and salt bridges found in the domain:domain interface by the crystallographic studies. These calculations yielded reasonable average energy terms for each interaction category.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
203
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
799-802
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Analysis of immunoglobulin domain interactions. Evidence for a dominant role of salt bridges.
pubmed:affiliation
Biological, Environmental, and Medical Research Division, Argonne National Laboratory, IL 60439-4833.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.