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

Kumar Pichumani; Gijo George; Sankeerth Hebbar; Bhaswati Chatterjee; Srinivasarao Raghothama

doi:10.1016/j.cplett.2015.03.048

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

Kumar Pichumani, Gijo George, Sankeerth Hebbar, Bhaswati Chatterjee, Srinivasarao Raghothama

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Abstract Longitudinal relaxation due to cross-correlation between dipolar (¹H^N-¹H^α) and amide-proton chemical shift anisotropy (¹H^N CSA) has been measured in a model tripeptide Piv-^LPro-^LPro-^LPhe-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.

Original language	English (US)
Article number	32894
Pages (from-to)	126-129
Number of pages	4
Journal	Chemical Physics Letters
Volume	627
DOIs	https://doi.org/10.1016/j.cplett.2015.03.048
State	Published - May 1 2015

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

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

abstract = "Abstract Longitudinal relaxation due to cross-correlation between dipolar (1HN-1Hα) and amide-proton chemical shift anisotropy (1HN CSA) has been measured in a model tripeptide Piv-LPro-LPro-LPhe-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.",

author = "Kumar Pichumani and Gijo George and Sankeerth Hebbar and Bhaswati Chatterjee and Srinivasarao Raghothama",

year = "2015",

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doi = "10.1016/j.cplett.2015.03.048",

language = "English (US)",

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pages = "126--129",

journal = "Chemical Physics Letters",

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T1 - Effects of hydrogen bonding on amide-proton chemical shift anisotropy in a proline-containing model peptide

AU - Pichumani, Kumar

AU - George, Gijo

AU - Hebbar, Sankeerth

AU - Chatterjee, Bhaswati

AU - Raghothama, Srinivasarao

PY - 2015/5/1

Y1 - 2015/5/1

N2 - Abstract Longitudinal relaxation due to cross-correlation between dipolar (1HN-1Hα) and amide-proton chemical shift anisotropy (1HN CSA) has been measured in a model tripeptide Piv-LPro-LPro-LPhe-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.

AB - Abstract Longitudinal relaxation due to cross-correlation between dipolar (1HN-1Hα) and amide-proton chemical shift anisotropy (1HN CSA) has been measured in a model tripeptide Piv-LPro-LPro-LPhe-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.

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DO - 10.1016/j.cplett.2015.03.048

M3 - Article

AN - SCOPUS:84927617938

SN - 0009-2614

VL - 627

SP - 126

EP - 129

JO - Chemical Physics Letters

JF - Chemical Physics Letters

M1 - 32894

ER -

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

Abstract

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