By the same authors

From the same journal

From the same journal

Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins

Research output: Contribution to journalArticle

Standard

Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins. / Perras, Frédéric A; Marion, Dominique; Boisbouvier, Jérôme; Bryce, David L; Plevin, Michael J.

In: Angewandte Chemie International Edition, 22.05.2017, p. 1-5.

Research output: Contribution to journalArticle

Harvard

Perras, FA, Marion, D, Boisbouvier, J, Bryce, DL & Plevin, MJ 2017, 'Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins', Angewandte Chemie International Edition, pp. 1-5. https://doi.org/10.1002/anie.201702626

APA

Perras, F. A., Marion, D., Boisbouvier, J., Bryce, D. L., & Plevin, M. J. (2017). Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins. Angewandte Chemie International Edition, 1-5. https://doi.org/10.1002/anie.201702626

Vancouver

Perras FA, Marion D, Boisbouvier J, Bryce DL, Plevin MJ. Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins. Angewandte Chemie International Edition. 2017 May 22;1-5. https://doi.org/10.1002/anie.201702626

Author

Perras, Frédéric A ; Marion, Dominique ; Boisbouvier, Jérôme ; Bryce, David L ; Plevin, Michael J. / Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins. In: Angewandte Chemie International Edition. 2017 ; pp. 1-5.

Bibtex - Download

@article{4c6ca3aa84824267809c0a54af8d9f53,
title = "Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins",
abstract = "Protein structure and function is dependent on myriad noncovalent interactions. Direct detection and characterization of these weak interactions in large biomolecules, such as proteins, is experimentally challenging. Herein, we report the first observation and measurement of long-range {"}through-space{"} scalar couplings between methyl and backbone carbonyl groups in proteins. These J couplings are indicative of the presence of noncovalent C-H⋅⋅⋅π hydrogen-bond-like interactions involving the amide π network. Experimentally detected scalar couplings were corroborated by a natural bond orbital analysis, which revealed the orbital nature of the interaction and the origins of the through-space J couplings. The experimental observation of this type of CH⋅⋅⋅π interaction adds a new dimension to the study of protein structure, function, and dynamics by NMR spectroscopy.",
keywords = "Journal Article",
author = "Perras, {Fr{\'e}d{\'e}ric A} and Dominique Marion and J{\'e}r{\^o}me Boisbouvier and Bryce, {David L} and Plevin, {Michael J}",
note = "{\circledC} 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.",
year = "2017",
month = "5",
day = "22",
doi = "10.1002/anie.201702626",
language = "English",
pages = "1--5",
journal = "Angewandte Chemie International Edition",
issn = "1433-7851",
publisher = "John Wiley and Sons Ltd",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins

AU - Perras, Frédéric A

AU - Marion, Dominique

AU - Boisbouvier, Jérôme

AU - Bryce, David L

AU - Plevin, Michael J

N1 - © 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.

PY - 2017/5/22

Y1 - 2017/5/22

N2 - Protein structure and function is dependent on myriad noncovalent interactions. Direct detection and characterization of these weak interactions in large biomolecules, such as proteins, is experimentally challenging. Herein, we report the first observation and measurement of long-range "through-space" scalar couplings between methyl and backbone carbonyl groups in proteins. These J couplings are indicative of the presence of noncovalent C-H⋅⋅⋅π hydrogen-bond-like interactions involving the amide π network. Experimentally detected scalar couplings were corroborated by a natural bond orbital analysis, which revealed the orbital nature of the interaction and the origins of the through-space J couplings. The experimental observation of this type of CH⋅⋅⋅π interaction adds a new dimension to the study of protein structure, function, and dynamics by NMR spectroscopy.

AB - Protein structure and function is dependent on myriad noncovalent interactions. Direct detection and characterization of these weak interactions in large biomolecules, such as proteins, is experimentally challenging. Herein, we report the first observation and measurement of long-range "through-space" scalar couplings between methyl and backbone carbonyl groups in proteins. These J couplings are indicative of the presence of noncovalent C-H⋅⋅⋅π hydrogen-bond-like interactions involving the amide π network. Experimentally detected scalar couplings were corroborated by a natural bond orbital analysis, which revealed the orbital nature of the interaction and the origins of the through-space J couplings. The experimental observation of this type of CH⋅⋅⋅π interaction adds a new dimension to the study of protein structure, function, and dynamics by NMR spectroscopy.

KW - Journal Article

U2 - 10.1002/anie.201702626

DO - 10.1002/anie.201702626

M3 - Article

SP - 1

EP - 5

JO - Angewandte Chemie International Edition

T2 - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

SN - 1433-7851

ER -