Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1995-11-13
|
| pubmed:abstractText |
The rotational relaxation times of the single tryptophan residues in endothelin-1, [Ala1,3,11,15]endothelin-1, human pro-endothelin-1, the linear hexapeptide Ac-His-Leu-Asp-Ile-Ile-Trp which corresponds to the C-terminal residues 16-21 in endothelin-1, the cyclic pentapeptide BQ123, and several di- and tri-peptides possessing C-terminal tryptophan residues have been determined from time-resolved fluorescence anisotropy decays obtained by phase/modulation techniques. Fluorescence lifetime distribution widths have also been examined as predictors of conformational heterogeneity/restriction. A significant contribution from a slow rotational component supports either the persistence, on the nano-second timescale at least, of a non-flexible alpha-helical structure for the C-terminal tail residues of endothelin-1 in water as solvent, as seen in the X-ray crystallographic structure, or the interaction of the C-terminal tail residues 16-21 with the constrained disulfide-bridged core residues 1-15. This slow rotational contribution is less evident in the linear, acyclic tetraalanine analogue but greatly increased in pro-endothelin-1. In BQ123 the fluorescence characteristics support the occurrence of a dominant rotameric form involving the indole sidechain of the D-tryptophan residue (C alpha-C beta torsion angle chi 1 of 60 degrees, as previously determined by NMR.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0367-8377
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
46
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
56-64
|
| pubmed:dateRevised |
2000-12-18
|
| pubmed:meshHeading |
pubmed-meshheading:7558597-Amino Acid Sequence,
pubmed-meshheading:7558597-Endothelins,
pubmed-meshheading:7558597-Fluorescence Polarization,
pubmed-meshheading:7558597-Molecular Sequence Data,
pubmed-meshheading:7558597-Peptides,
pubmed-meshheading:7558597-Protein Conformation,
pubmed-meshheading:7558597-Tryptophan
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Solution conformational dynamics of the C-terminal residues in endothelin-1 and some analogues: a time-resolved fluorescence study.
|
| pubmed:affiliation |
Marion Merrell Dow Research Center, Strasbourg, France.
|
| pubmed:publicationType |
Journal Article
|