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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|
|Authors: ||BOBDE V|
|Keywords: ||secondary structure|
|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.|
|Appears in Collections:||Article|
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