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

Autor:	Sankeerth Hebbar, Srinivasarao Raghothama, Gijo George, Bhaswati Chatterjee, Kumar Pichumani
Rok vydání:	2015
Předmět:	chemistry.chemical_classification chemistry Hydrogen bond Stereochemistry Intramolecular force Relaxation (NMR) General Physics and Astronomy Peptide bond Peptide Tripeptide Physical and Theoretical Chemistry Isomerization Cis–trans isomerism
Zdroj:	Chemical Physics Letters. 627:126-129
ISSN:	0009-2614
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::37c4bdc0ddf93339c04b5ef14845792d https://doi.org/10.1016/j.cplett.2015.03.048 Zobrazit plný text záznamu Full Text from ScienceDirect