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A SINGLE-POINT CHIRAL INVERSION THAT SELFORGANIZES A RANDOMCOIL PEPTIDE - APOLAR SOLVENT CONFORMATION OF BOC-(L-BACKSLASH-D)-GLU-ALA-LEU-LYSNHME

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Title A SINGLE-POINT CHIRAL INVERSION THAT SELFORGANIZES A RANDOMCOIL PEPTIDE - APOLAR SOLVENT CONFORMATION OF BOC-(L-BACKSLASH-D)-GLU-ALA-LEU-LYSNHME
 
Creator BOBDE, V
BERI, S
RAWALE, S
SATYANARAYANA, CVV
DURANI, S
 
Subject alpha-helix formation
stabilization
templates
proteins
alanine
water
model
glu
 
Description The tetrapeptide Boc-L-Glu-Ala-Leu-LysNHMe (1) reveals a random coil conformation, based on its Glu(gamma) and Lys(epsilon) methylene proton aniosotropic shift, GluNH chemical shift, NOEs in chloroform-DMSO (6:1), and its amide proton temperature coefficients in DMSO, while on similar considerations, the diastereomer Boc-D-Glu-Ala-Leu-LysNHMe (2) is characterized as a highly ordered 3/10 type distorted protohelix with a remarkably stable intramolecular salt bridge under these solvent conditions.
 
Publisher PERGAMON-ELSEVIER SCIENCE LTD
 
Date 2011-08-23T09:40:35Z
2011-12-26T12:56:24Z
2011-12-27T05:45:06Z
2011-08-23T09:40:35Z
2011-12-26T12:56:24Z
2011-12-27T05:45:06Z
1995
 
Type Article
 
Identifier TETRAHEDRON, 51(10), 3077-3086
0040-4020
http://dx.doi.org/10.1016/0040-4020(95)00047-C
http://dspace.library.iitb.ac.in/xmlui/handle/10054/10475
http://hdl.handle.net/10054/10475
 
Language en