Linked Life Data

9230473

Source:http://linkedlifedata.com/resource/pubmed/id/9230473

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-9-4
pubmed:abstractText
The conformational preferences of peptide T (ASTTTNYT) were analysed by means of computational methods. A thorough exploration of the conformational space was carried out within the framework of the molecular mechanics approach, using simulated annealing as a searching strategy. Specifically, in order to obtain a subset of low-energy conformations with energies close to the global minimum as complete as possible, a simulated annealing protocol was repeated several times in a recursive fashion. The results of the search indicate that the peptide exhibits a alpha-helical character although most of the conformations characterized, including the global minimum, can be described as bent conformations. Conformations exhibiting beta-turn motives previously proposed from NMR studies were also characterized, although they are not very predominant in the set of low-energy conformations.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1075-2617
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
85-92
pubmed:dateRevised
2001-11-13
pubmed:meshHeading
pubmed:articleTitle
Computational study of the conformational domains of peptide T.
pubmed:affiliation
Istituto di Biochimica delle Macromolecole, Seconda Università degli Studi di Napoli, Italy.
pubmed:publicationType
Journal Article