| pubmed-article:15895435 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15895435 | lifeskim:mentions | umls-concept:C0441635 | lld:lifeskim |
| pubmed-article:15895435 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:15895435 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:15895435 | lifeskim:mentions | umls-concept:C0031453 | lld:lifeskim |
| pubmed-article:15895435 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:15895435 | lifeskim:mentions | umls-concept:C1704973 | lld:lifeskim |
| pubmed-article:15895435 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:15895435 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:15895435 | lifeskim:mentions | umls-concept:C0772162 | lld:lifeskim |
| pubmed-article:15895435 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15895435 | pubmed:dateCreated | 2005-11-10 | lld:pubmed |
| pubmed-article:15895435 | pubmed:abstractText | The incporation of beta-amino acid residues into the strand segments of designed beta-hairpin leads to the formation of polar sheets, since in the case of beta-peptide strands, all adjacent carbonyl groups point in one direction and the amide groups orient in the opposite direction. The conformational analysis of two designed peptide hairpins composed of alpha/beta-hybrid segments are described: Boc-Leu-betaPhe-Val-(D)-Pro-Gly-Leu-betaPhe-Val-OMe (1) and Boc-betaLeu-Phe-betaVal-D-Pro-Gly-betaLeu-Phe-betaVal-OMe (2). A 500-MHz 1H-NMR (nuclear magnetic resonance) analysis in methanol supports a significant population of hairpin conformations in both peptides. Diagnostic nuclear Overhauser effects (NOEs) are observed in both cases. X-ray diffraction studies on single crystals of peptide 1 reveal a beta-hairpin conformation in both the molecules, which constitute the crystallographic asymmetric unit. Three cross-strand hydrogen bonds and a nucleating type II' beta-turn at the D-Pro-Gly segment are observed in the two independent molecules. In peptide 1, the betaPhe residues at positions 2 and 7 occur at the nonhydrogen-bonding position, with the benzyl side chains pointing on opposite faces of the beta-sheet. The observed aromatic centroid-to-centroid distances are 8.92 A (molecule A) and 8.94 A (molecule B). In peptide 2, the aromatic rings must occupy facing positions in antiparallel strands, in the NMR-derived structure. Peptide 1 yields a normal "hairpin-like" CD spectrum in methanol with a minimum at 224 nm. The CD spectrum of peptide 2 reveals a negative band at 234 nm and a positive band at 221 nm, suggestive of an exciton split doublet. Modeling of the facing Phe side chains at the hydrogen-bonding position of a canonical beta-hairpin suggests that interring separation is approximately 4.78 A for the gauche+ gauche- (g+ g-) rotamer. A previously reported peptide beta-hairpin composed of only alpha-amino acids, Boc-Leu-Phe-Val-D-Pro-Gly-Leu-Phe-Val-OMe also exhibited an anomalous far-UV (ultraviolet) CD (circular dichroism) spectrum, which was interpreted in terms of interactions between facing aromatic chromophores, Phe 2 and Phe 7 (C. Zhao, P. L. Polavarapu, C. Das, and P. Balaram, Journal of the American Chemical Society, 2000, Vol 122, pp. 8228-8231). | lld:pubmed |
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| pubmed-article:15895435 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15895435 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15895435 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15895435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15895435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15895435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15895435 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15895435 | pubmed:issn | 0006-3525 | lld:pubmed |
| pubmed-article:15895435 | pubmed:author | pubmed-author:RaghothamaSS | lld:pubmed |
| pubmed-article:15895435 | pubmed:author | pubmed-author:GopiHosahudya... | lld:pubmed |
| pubmed-article:15895435 | pubmed:author | pubmed-author:BalaramPadman... | lld:pubmed |
| pubmed-article:15895435 | pubmed:author | pubmed-author:KarleIsabella... | lld:pubmed |
| pubmed-article:15895435 | pubmed:author | pubmed-author:GilardiRichar... | lld:pubmed |
| pubmed-article:15895435 | pubmed:author | pubmed-author:RoyRituparna... | lld:pubmed |
| pubmed-article:15895435 | pubmed:copyrightInfo | Copyright 2005 Wiley Periodicals, Inc. | lld:pubmed |
| pubmed-article:15895435 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15895435 | pubmed:volume | 80 | lld:pubmed |
| pubmed-article:15895435 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15895435 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15895435 | pubmed:pagination | 787-99 | lld:pubmed |
| pubmed-article:15895435 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15895435 | pubmed:meshHeading | pubmed-meshheading:15895435... | lld:pubmed |
| pubmed-article:15895435 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15895435 | pubmed:articleTitle | Peptide hairpins with strand segments containing alpha- and beta-amino acid residues: cross-strand aromatic interactions of facing Phe residues. | lld:pubmed |
| pubmed-article:15895435 | pubmed:affiliation | Molecular Biophysics Unit, Indian Institute of Science, Bangalore-560012, India. | lld:pubmed |
| pubmed-article:15895435 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15895435 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15895435 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:15895435 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15895435 | lld:pubmed |
