Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-1-5
pubmed:abstractText
The energy of binding between proteins may be seen as the sum of the contributions of the individual amino acid residues. These contributions are additive when the binding energy, due to different amino acid residues, is independent of the interactions between amino acids in the same polypeptide chain. A measure of non-additivity is the coupling free energy. In this communication it is shown that: (1) the coupling free energy is the sum of intramolecular and intermolecular contributions; and (2), when additivity exists, experimentally determined values for the free energy of transfer of amino acids from water to the hydrophobic protein-protein interface are a very good approximation of their contribution to the energy of binding. Additivity cycles can be useful in determining the precise conditions where this approximation holds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
196
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
733-5
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Non-additivity in protein-protein interactions.
pubmed:affiliation
Department of Biological Chemistry, Hebrew University of Jerusalem, Israel.
pubmed:publicationType
Journal Article