Linked Life Data

16453362

Source:http://linkedlifedata.com/resource/pubmed/id/16453362

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2006-4-11
pubmed:abstractText
The effects of inserting unsubstituted omega-amino acids into the strand segments of model beta-hairpin peptides was investigated by using four synthetic decapeptides, Boc-Leu-Val-Xxx-Val-D-Pro-Gly-Leu-Xxx-Val-Val-OMe: peptide 1 (Xxx=Gly), peptide 2 (Xxx=betaGly=betahGly=homoglycine, beta-glycine), peptide 3 (Xxx=gammaAbu=gamma-aminobutyric acid), peptide 4 (Xxx=deltaAva=delta-aminovaleric acid). 1H NMR studies (500 MHz, methanol) reveal several critical cross-strand NOEs, providing evidence for beta-hairpin conformations in peptides 2-4. In peptide 3, the NMR results support the formation of the nucleating turn, however, evidence for cross-strand registry is not detected. Single-crystal X-ray diffraction studies of peptide 3 reveal a beta-hairpin conformation for both molecules in the crystallographic asymmetric unit, stabilized by four cross-strand hydrogen bonds, with the gammaAbu residues accommodated within the strands. The D-Pro-Gly segment in both molecules (A,B) adopts a type II' beta-turn conformation. The circular dichroism spectrum for peptide 3 is characterized by a negative CD band at 229 nm, whereas for peptides 2 and 4, the negative band is centered at 225 nm, suggesting a correlation between the orientation of the amide units in the strand segments and the observed CD pattern.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-11169393, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-11259666, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-11686719, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-11710070, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-11740924, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-11880601, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-14967024, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-15148683, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-7488115, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-8710845, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-8946799, http://linkedlifedata.com/resource/pubmed/commentcorrection/16453362-9163422
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0947-6539
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3295-302
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Hybrid peptide hairpins containing alpha- and omega-amino acids: conformational analysis of decapeptides with unsubstituted beta-, gamma-, and delta-residues at positions 3 and 8.
pubmed:affiliation
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural