Residue dependent hydrogen-bonding preferences in orthanilic acid-based short peptide β-turn motifs. Issue 42 (11th April 2016)

• Record Type: Journal Article
• Authors: Jedhe, Ganesh S.; Vijayadas, Kuruppanthara N.; Kotmale, Amol S.; Sangtani, Ekta; Shinde, Dinesh R.; Gonnade, Rajesh G.; Rajamohanan, Pattuparambil R.; Sanjayan, Gangadhar J.
• Is Part Of: RSC advances. Volume 6:Issue 42(2016)
• Page Start: 35328
• Page End: 35331
• Publication Date: 2016-04-11
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c6ra05684a
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : This communication describes the competition between native β-turn (C10) and 2-aminobenzenesulfonic acid ( S Ant)(orthanilic acid)-based pseudo β-turn (C11) in their hybrid peptides. Abstract : This communication describes the competition between native β-turn (C10) and 2-aminobenzenesulfonic acid ( S Ant)(orthanilic acid)-based pseudo β-turn (C11) in their hybrid peptides. Solid-state crystal structure and solution-state NMR studies revealed that C10 and C11 can be simultaneously observed under appropriate conditions. The variable temperature NMR coefficient data suggest that the isolated C11/C14 hydrogen bond is weaker in comparison with the consecutive C10 and C11 turns.