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HARNESSING D-AMINO ACIDS FOR PEPTIDE MOTIF DESIGNS - SYNTHESIS AND SOLUTION CONFORMATION OF BOC-D-GLU-ALA-GLY-LYS-NHME AND BOC-L-GLU-ALA-GLY-LYS-NHME

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Title HARNESSING D-AMINO ACIDS FOR PEPTIDE MOTIF DESIGNS - SYNTHESIS AND SOLUTION CONFORMATION OF BOC-D-GLU-ALA-GLY-LYS-NHME AND BOC-L-GLU-ALA-GLY-LYS-NHME
 
Creator BOBDE V
SASIDHAR, YU
DURANI, S
 
Subject secondary structure
denovo design
alpha-helices
salt bridges
proteins
water
stabilization
fragments
templates
residues
beta-turns
d-amino acid
electrostatically stabilized peptides
3(10)-helical conformation
helix design
salt bridges
 
Description In examining the use of D-amino acids in designing specific peptide folding motifs, the tetrapeptide Boc-D-Glu-Ala-Gly-Lys-NHMe 1 and its analog 2 featuring L-Glu were synthesized for a comparison of their solution conformations by NMR spectroscopy. The temperature coefficients of amide proton resonances, NOE data, side-chain CH2 anisotropies and salt titration results suggest a weak type II reverse-turn conformation for peptide 2, and a tandem type II' turn-3(10)-helix conformation of appreciable conformational stability for peptide I in apolar solvents. The latter is of potential interest as the N-terminal helix cap that could support the design of longer 3(10) helices. Possible origins of appreciable difference in the conformational stabilities of the diastereomers are discussed. (C) Munksgaard 1994.
 
Publisher BLACKWELL MUNKSGAARD
 
Date 2011-07-19T02:07:55Z
2011-12-26T12:50:57Z
2011-12-27T05:37:11Z
2011-07-19T02:07:55Z
2011-12-26T12:50:57Z
2011-12-27T05:37:11Z
1994
 
Type Article
 
Identifier INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH, 43(3), 209-218
0367-8377
http://dspace.library.iitb.ac.in/xmlui/handle/10054/5141
http://hdl.handle.net/10054/5141
 
Language en