Linked Life Data

2081267

Source:http://linkedlifedata.com/resource/pubmed/id/2081267

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11-12
pubmed:dateCreated
1991-5-9
pubmed:abstractText
Molecular dynamics simulations on the transmembrane antibiotic peptide alamethicin have been performed in the NVT ensemble (i.e., the number of particles N, the volume V, and the temperature T of the system are kept constant). Results on the structure and conformational flexibility of this molecule are discussed and compared with previous experimental CD, x-ray, nmr data and theoretical computations on fragments analogues. An extensive study of structural and dynamic properties from H-bonding pattern analysis is presented. Evidences for a largely alpha-helix structure with some extent of freedom in the C-terminal region are found. Further, a partition of the molecule into three regions on the base of structural features and dynamic behavior has been proposed, and the correlation among the motions of the three regions is described.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0006-3525
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1083-99
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Restrained and unrestrained molecular dynamics simulations in the NVT ensemble of alamethicin.
pubmed:affiliation
Department of Biochemistry, University of Oxford, United Kingdom.
pubmed:publicationType
Journal Article