Observation of a 3 10- / alpha- Helical Transition upon Sequence Permutation", Biopolymers 31, 1763-1774 (1991).ģ) Basu, G. "Conformational Preferences of Oligopeptides Rich in alpha-aminoisobutyric Acid.
"Long-Range Electronic Interactions in Peptides: The Remote Heavy Atom Effect", J. THEORETICAL AND EXPERIMENTAL STUDY OF 3 10-HELIXġ) Basu, G., Kubasik, M., Anglos, D., Secor, B. STRUCTURAL AND SEQUENCE PATTERNS OF INTEGRAL MEMBRANE PROTEINSĮLECTROSTATIC SIGNATURES IN ADENINE AND GUANINE BINDING SITES IN PROTEINS
#Aib kubasik jmol free
These designed peptide helices have been used for:ġ) Quantitative comparison of helix forming free energies of Ala and Aib, using the Zimm-Bragg model.Ģ) Identifying artifacts (arising from interfering aromatic side chain contributions) in far-UVCD-monitored peptide unfolding profiles.ģ) Designing helical scaffolds (in collaboration with Prof. Using a-amino isobutyric acid (Aib) as a strong helix forming amino acid, we have designed and synthesized water soluble peptides that show substantial helicity at ambient temperatures. This work has important implications in understanding protein folding initiation sites in proteins. The work is in its preliminary stage, however, our results indicate that some of the peptides can show turn like secondary structure in isolation. The solution conformations of these peptides were studied by NMR and CD spectroscopy.
#Aib kubasik jmol series
The work has fundamental importance in understanding factors responsible for unique three dimensional structures of proteins.Ī series of short peptides were synthesized that exhibit the 3 10-helical conformation in proteins. In addition, neural network methodology was used to predict 3 10-helices in proteins. This includes, identification of supersecondary structural motifs containing long 3 10-helices, classification and analysis of shortest protein helices, and, estimation of conformational entropy of protein helices as a function of helix length. Investigated the solution conformation (NMR) of a 20-residue peptide fragment from Protein A that showed important immunological properties.įrom known protein structures in the protein data bank, a detailed analysis of protein 3 10-helices has been completed. The results will help in identifying amino acids that can be mutated for improving the nutritional content of mustard seeds.
Tel :+81-743-72-5391 (from outside Japan)įax :+81-743-72-5391 (from outside Japan)ĭeveloped a theoretical model that relates protein electron transfer rate and protein dynamics with application on cytochrome c.Ĭompleted rigorous solution structural analysis and equilibrium unfolding, by CD and fluorescence spectroscopy, of a 2S seed albumin from Brassica juncea (mustard seeds). Postdoctoral Fellow: Kyoto University, 1993-1995Ĩ916-5 Takayama, Ikoma, Nara 630-01, JAPAN Visiting Scientist: Temple University, 2000 June-Aug Visiting Scientist: Memorial Sloan Ketering Cancer Center, 1998 Oct-Dec Lecturer: Bose Institute, Calcutta, India, 1995. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.Last updated: SeptemGautam Basu Adjunct Associate Professor The aggregation phenomenon is mainly due to hydrophobic interactions occurring between very stable helical structures, and the aromatic groups in the peptides seem to play a minor role. Atomic force microscopy images indicate that these aggregates promote formation of long fibrils once they are deposited on a mica surface. On the other hand, the homologous peptide with 15 U forms very stable and compact aggregates in 70/30 (v/v) methanol/water solution. Spectroscopic experiments and molecular dynamics simulations show that the shortest homo-peptide, constituted by six U, does not exhibit any tendency to aggregate under the conditions examined. The peptides investigated have chain lengths between six and 15 residues and comprise benzyl and naphthyl groups at the N- and C-termini, respectively. In the present article, the aggregation properties of the homo-peptides formed by α-aminoisobutyric acid (U) residues are discussed. Interactions between peptides are relevant from a biomedical point of view, in particular for the role played by their aggregates in different important pathologies, and also because peptide aggregates represent promising scaffolds for innovative materials.
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