ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Effects of hydrogen bonding on amide-proton chemical shift anisotropy in a proline-containing model peptide

Pichumani, Kumar and George, Gijo and Hebbar, Sankeerth and Chatterjee, Bhaswati and Raghothama, Srinivasarao (2015) Effects of hydrogen bonding on amide-proton chemical shift anisotropy in a proline-containing model peptide. In: CHEMICAL PHYSICS LETTERS, 627 . pp. 126-129.

[img] PDF
che_phy_let-627_126_2015.pdf - Published Version
Restricted to Registered users only

Download (589kB) | Request a copy
Official URL: http://dx.doi.org/10.1016/j.cplett.2015.03.048

Abstract

Longitudinal relaxation due to cross-correlation between dipolar ((HN-1H alpha)-H-1) and amide-proton chemical shift anisotropy (H-1(N) CSA) has been measured in a model tripeptide Piv-(L)Pro-(L)Pro-(L)Phe-OMe. The peptide bond across diproline segment is known to undergo cis/trans isomerization and only in the cis form does the lone Phe amide-proton become involved in intramolecular hydrogen bonding. The strength of the cross correlated relaxation interference is found to be significantly different between cis and trans forms, and this difference is shown as an influence of intramolecular hydrogen bonding on the amide-proton CSA. (C) 2015 Elsevier B.V. All rights reserved.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
Keywords: CROSS-CORRELATED RELAXATION; NUCLEAR-MAGNETIC-RESONANCE; STATE NMR-SPECTROSCOPY; DIPROLINE TEMPLATES; SECONDARY STRUCTURE; DESIGNED PEPTIDES; TENSORS; PROTEINS; DIPOLAR; SOLIDS
Department/Centre: Division of Chemical Sciences > NMR Research Centre (Formerly Sophisticated Instruments Facility)
Depositing User: Id for Latest eprints
Date Deposited: 22 May 2015 07:16
Last Modified: 22 May 2015 07:16
URI: http://eprints.iisc.ac.in/id/eprint/51552

Actions (login required)

View Item View Item