Linked Life Data

7577910

Source:http://linkedlifedata.com/resource/pubmed/id/7577910

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
1995-12-14
pubmed:abstractText
Whether hydrogen bonds between side chains are energetically significant in proteins and peptides has been controversial. A method is given here for measuring these interactions in peptide helices by comparing the helix contents of peptides with 1, 2, or 3 interactions. Results are given for the glutamine--aspartate (i, i + 4) hydrogen-bond interaction. The Gibbs energy of the interaction is -1.0 kcal/mol when aspartate is charged and -0.4(4) kcal/mol when it is protonated. Magnetic resonance experiments show that the aspartate carboxylate group interacts specifically with the trans amide proton (HE) of glutamine. The interaction is observed only when the glutamine residue is N-terminal to the aspartate and when the spacing is (i, i + 4). The same stereochemistry is found in protein structures, where the (i, i + 4) glutamine-aspartate interaction occurs much more frequently than other possible arrangements.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13267-71
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Measuring the strength of side-chain hydrogen bonds in peptide helices: the Gln.Asp (i, i + 4) interaction.
pubmed:affiliation
Department of Biochemistry, Beckman Center, Stanford Medical Center, California 94305-5307, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.