Linked Life Data

19624237

Source:http://linkedlifedata.com/resource/pubmed/id/19624237

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-7-23
pubmed:abstractText
Intramolecular hydrogen bonding in the Pro-Ala-Pro and Pro-Phe-Pro tripeptides has been characterized using Bader's atoms in molecule (AIM) analyses of relevant electron density topologies. The properties of hydrogen bonds with corresponding ring strains were investigated. Good correlations along the decrease in electron densities at ring critical points were examined from five- to ten-membered hydrogen-bound ring sizes; seven-membered rings being the most energetically favored. AIM analysis confirms the logical conclusion that the molecule has to become very compact to form as many hydrogen bonds as possible. The relatively large hydrogen bond stabilization attributed to the pronounced network of interactions comes at the "energetic expense" of a relatively large internal repulsion due to the compactness of the structures. The net balanced result was a very modest increase in the zero point corrected conformation energy (DeltaE(ZPEC)). These findings aid in establishing hydrogen bonding rules in reductionist "bottoms-up" approaches to peptide and protein folding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1089-7690
pubmed:author
pubmed:issnType
Electronic
pubmed:day
21
pubmed:volume
131
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
035105
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Network of hydrogen bonds in Pro-Ala-Pro and Pro-Phe-Pro diamides: a first principles study of Ala-->Phe point mutation in proline environment.
pubmed:affiliation
College of Chemistry, Beijing Normal University, Xin Wai Street 19, Hai Dian, Beijing 100875, China. huiw81@mail.bnu.edu.cn
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't