P
Padmanabhan Balaram
Researcher at Indian Institute of Science
Publications - 501
Citations - 17151
Padmanabhan Balaram is an academic researcher from Indian Institute of Science. The author has contributed to research in topics: Peptide & Helix. The author has an hindex of 63, co-authored 499 publications receiving 16563 citations. Previous affiliations of Padmanabhan Balaram include National Centre for Biological Sciences & Council of Scientific and Industrial Research.
Papers
More filters
Journal ArticleDOI
Conformations of dehydrophenylalanine containing peptides: nmr studies of an acyclic hexapeptide with two delta Z-Phe residues.
TL;DR: The results suggest that Δz‐Phe residues do not provide compelling conformational constraints and suggest a significant solvent‐dependent conformational variability in acyclic dehydrophenylalanine.
Journal ArticleDOI
Conformations of dehydrophenylalanine containing peptides. NMR studies on three tripeptides with a central dehydrophenylalanyl residue.
TL;DR: In this article, three tripeptides containing a central Z-dehydrophenylalanine residue (Δz-Phe) were synthesized and their solution conformations investigated by 270 MHz 1H NMR spectroscopy.
Journal ArticleDOI
Proteolytic stability of β-peptide bonds probed using quenched fluorescent substrates incorporating a hemoglobin cleavage site
Hosahudya N. Gopi,Gudihal Ravindra,Prajna P Pal,Priyaranjan Pattanaik,Hemalatha Balaram,Padmanabhan Balaram +5 more
TL;DR: Fluorescence and mass spectral measurements demonstrate that the insertion of an β‐residues at the potential cleavage sites completely abolishes the action of proteases.
Journal ArticleDOI
Membrane channel forming polypeptides. 270-MHz proton magnetic resonance studies of the aggregation of the 11-21 fragment of suzukacillin in organic solvents.
M. Iqbal,Padmanabhan Balaram +1 more
TL;DR: It is established that replacement of Gln by Ala is without effect on backbone conformation, and a major role for the Gln side chain in peptide association is suggested by differences in the NMR behavior of the GlN(1) and Ala(1), which shows evidence for intermolecular interactions.
Journal ArticleDOI
Tuning the beta-turn segment in designed peptide beta-hairpins: construction of a stable type I' beta-turn nucleus and hairpin-helix transition promoting segments.
TL;DR: In this paper, Boc-Leu-Phe-val-Val-Aib and Leu-Val Val-OMe (3b) have been investigated to construct models of a stable type I' β-turn nucleated hairpin and to generate systems for investigating helix-hairpin conformational transitions.