Linked Life Data

38217

Source:http://linkedlifedata.com/resource/pubmed/id/38217

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1979-10-24
pubmed:abstractText
The 13C spectra of the linear tripeptidyl diastereoisomers, Gly-Gly-Leu, Gly-Gly-D-Leu, Leu-Gly-Gly, D-Leu-Gly-Gly, Ala3, Ala-Ala-D-Ala, Ala-D-Ala-Ala, Val3, and Val-Val-D-Val are very similar or even identical at pH meter readings of 1.0, 7.0 and 12.0 in D2O. The spectra of Pro-Leu-Gly-NH2 and Pro-D-Leu-Gly-NH2 likewise show only minor differences in 13C chemical shifts (less than 0.4 p.p.m.) under similar conditions. This contrasts significantly with previous findings comparing 13C chemical shifts of cyclo(Pro-Leu) and cyclo(Pro-D-Leu) where major differences in chemical shifts were observed for both residues due to differences in conformational constraints present in these cyclic proline-containing peptides. The least-squares fit of spin-lattice relaxation times (T1) for Pro-Leu-Gly-NH2 and Pro-D-Leu-Gly-NH2 show that it is not possible to fit all the T1 values to a unique and rigid structure whether folded or extended. The glycyl residue undergoes enhanced motion when compared with the prolyl and leucyl residues. Internal motion must be postulated within the proline ring and for the CH3 groups of leucine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0367-8377
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
473-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Effects of D and L amino acid residues in linear peptides on carbon-13 nuclear magnetic resonance parameters.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.