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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/5141

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
Authors: BOBDE V
SASIDHAR, YU
DURANI, S
Keywords: secondary structure
denovo design
alpha-helices
salt bridges
proteins
water
stabilization
fragments
templates
residues
Issue Date: 1994
Publisher: BLACKWELL MUNKSGAARD
Citation: INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH, 43(3), 209-218
Abstract: 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.
URI: http://dspace.library.iitb.ac.in/xmlui/handle/10054/5141
http://hdl.handle.net/10054/5141
ISSN: 0367-8377
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