Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Kuruppanthara N. Vijayadas"'
Autor:
Kuruppanthara N. Vijayadas, K. N. Chaitanya, Rajesh G. Gonnade, Tukaram S. Ingole, Amol S. Kotmale, Gangadhar J. Sanjayan, P. R. Rajamohanan, Rupesh L. Gawade
Publikováno v:
European Journal of Organic Chemistry. 2016:1380-1388
Autor:
Kuruppanthara N. Vijayadas, Gangadhar J. Sanjayan, Rajesh G. Gonnade, Dinesh R. Shinde, Pattuparambil R. Rajamohanan, Ekta Sangtani, Amol S. Kotmale, Ganesh S. Jedhe
Publikováno v:
RSC Advances. 6:35328-35331
This communication describes the competition between native β-turn (C10) and 2-aminobenzenesulfonic acid (SAnt)(orthanilic acid)-based pseudo β-turn (C11) in their hybrid peptides. Solid-state crystal structure and solution-state NMR studies reveal
Publikováno v:
European Journal of Organic Chemistry. 2014:7763-7780
Chemists' constant pursuit of understanding of the underlying principles of nature's most intricate phenomenon such as protein folding has led to the development of the field of “foldamers”. The emergence of diverse classes of unnatural amino aci
Autor:
Rajesh G. Gonnade, Veera V. E. Ramesh, Vijaykumar H. Thorat, Pattuparambil R. Rajamohanan, Roshna V. Nair, Tukaram S. Ingole, Kuruppanthara N. Vijayadas, Hilda C. Davis, Gangadhar J. Sanjayan, Panchami Prabhakaran, Rupesh L. Gawade, Sangram S. Kale, Vedavati G. Puranik
Publikováno v:
European Journal of Organic Chemistry. 2013:3529-3542
This article details the characteristic conformational features of the Ant-Pro reverse turn ― a folded pseudo β-turn motif that displays a closed nine-membered-ring hydrogen-bonded network involving just two amino acid residues, namely anthranilic
Publikováno v:
ChemInform. 46
Chemists' constant pursuit of understanding of the underlying principles of nature's most intricate phenomenon such as protein folding has led to the development of the field of “foldamers”. The emergence of diverse classes of unnatural amino aci
Autor:
Rajesh G. Gonnade, Kuruppanthara N. Vijayadas, Amol S. Kotmale, Gangadhar J. Sanjayan, Shridhar H. Thorat, Pattuparambil R. Rajamohanan, Roshna V. Nair
Publikováno v:
Organicbiomolecular chemistry. 13(10)
This communication depicts an intriguing example of hydrogen-bonding reversal upon introduction of a sulfonamide linkage at the N-terminus of a synthetic reverse-turn peptide motif. The ready availability of two sulfonyl oxygen atoms, as hydrogen-bon
Autor:
Gangadhar J. Sanjayan, Rajesh G. Gonnade, Kuruppanthara N. Vijayadas, Amol S. Kotmale, Roshna V. Nair, Pattuparambil R. Rajamohanan, Panchami Prabhakaran, Vedavadi G. Puranik, Rupesh L. Gawade
Publikováno v:
Organicbiomolecular chemistry. 11(48)
Although known for their inferiority as hydrogen-bonding acceptors when compared to amides, esters are often found at the C-terminus of peptides and synthetic oligomers (foldamers), presumably due to the synthetic readiness with which they are obtain
Autor:
Arup Roy, Vedavati G. Puranik, Rajesh G. Gonnade, Panchami Prabhakaran, Kuruppanthara N. Vijayadas, Gangadhar J. Sanjayan, Amol M. Kendhale, Veera V. E. Ramesh
Publikováno v:
Organicbiomolecular chemistry. 9(2)
This communication describes the development of conformationally constrained unnatural aromatic amino acids, constructed on rigid backbone wherein the carboxyl and amino groups project in two dimensions (planes) on the aromatic framework. Such a feat
Autor:
Rajesh G. Gonnade, Gangadhar J. Sanjayan, Veera V. E. Ramesh, Kuruppanthara N. Vijayadas, Snehal A. Dhokale, Pattuparambil R. Rajamohanan
Publikováno v:
Organic & Biomolecular Chemistry. 11:7072
This communication describes the folding propensity of a heterofoldamer motif featuring proline (Pro) and anthranilic acid (Ant) residues in a 1 : 2 : 1 (α : β : α) constitutional ratio. Structural investigations unequivocally suggest that the hyd
Autor:
Vedavadi G. Puranik, Hilda C. Davis, Kuruppanthara N. Vijayadas, Pattuparambil R. Rajamohanan, Amol S. Kotmale, Rupesh L. Gawade, Gangadhar J. Sanjayan
Publikováno v:
Chemical Communications. 48:9747
Two folded peptides featuring carboxamide and sulfonamide at the core of the peptide fold have been shown to possess almost similar conformational features, despite the well-known fact that carboxamides and sulfonamides have strikingly different hydr