Linked Life Data

8250906

Source:http://linkedlifedata.com/resource/pubmed/id/8250906

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-1-4
pubmed:abstractText
To elucidate the alpha-helix-stabilizing effect of amino acids at the helical ends, we prepared analogs of C-terminal fragments of neuropeptide Y (NPY) containing an alpha-helical part. The helix-stabilizing tendency of N-terminal amino acid in NPY (12-36) was found to be as follows: Thr > Ser > Gly > Gln > Cys > Asn > Asp > Val > Phe > Glu > Lys > Tyr > Ala = Trp > His > Arg, suggesting the importance of end capping. The capping effect was not evident when N-termini in NPY (11-36) and NPY (13-36) were replaced. Under the same conditions as those for the receptor binding, [Thr12]NPY (12-36) had about 4-fold higher alpha-helix content than [Arg12]NPY (12-36). However, there was no apparent relationship between the helix content and binding affinity to the Y2 receptor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
196
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1490-5
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Stabilization of alpha-helix in C-terminal fragments of neuropeptide Y.
pubmed:affiliation
Government Industrial Research Institute, Osaka, Japan.
pubmed:publicationType
Journal Article