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Direct observation of Calpha-Halpha...O=C hydrogen bonds in proteins by interresidue h3JCalphaC' scalar couplings

Cordier, Florence and Barfield, Michael and Grzesiek, Stephan. (2003) Direct observation of Calpha-Halpha...O=C hydrogen bonds in proteins by interresidue h3JCalphaC' scalar couplings. Journal of the American Chemical Society, 125 (51). pp. 15750-15751.

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Official URL: http://edoc.unibas.ch/dok/A5258790

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Abstract

The role of C−H···O hydrogen bonds in the stabilization of biomolecules is increasingly being recognized from the evidence of close C−H···O contacts in crystal structures. However, relatively little is known about their strength. Here, we report the observation of NMR scalar couplings (h3JCαC‘) between the two carbons on each side of Cα−Hα···O=C H-bonds in proteins. These couplings give direct evidence of the correlation of the electronic wave functions in the donor and acceptor groups of Cα−Hα···O=C H-bonds. A long-range H(NCO)CA experiment or a selective long-range H(NCA)CO experiment was used for the detection of h3JCαC‘ correlations in the β-sheet regions of the immunoglobulin binding domain of protein G. In total, six such correlations were detectable. These correspond to half of the Cα−Hα···O=C H-bonds of protein G with Hα···O distances shorter than 2.5 Å. The h3JCαC‘ couplings range from 0.2 to 0.3 Hz and are in good agreement with predicted average values based on DFT/FPT calculations. An anticorrelation is observed with the size of h3JNC‘ coupling constants across N−HN···O=C H-bonds, which share the same acceptor carbonyl oxygen.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Grzesiek)
UniBasel Contributors:Grzesiek, Stephan
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:American Chemical Society
ISSN:0002-7863
e-ISSN:1520-5126
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:28 Feb 2019 10:34
Deposited On:22 Mar 2012 13:21

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