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Structural dependencies of protein backbone ² J _NC' couplings

Nenad Jurani¹, J.J. Dannenberg², Gabriel Cornilescu³, Pedro Salvador⁴, Elena Atanasova⁵, Hee-Chul Ahn^3,6, Slobodan Macura¹, John L. Markley³, and Franklyn G. Prendergast^1,5

¹ Department of Biochemistry and Molecular Biology, Mayo Clinic and Foundation, Rochester, Minnesota, 55905, USA
² Department of Chemistry, City University of New York, Hunter College and the Graduate School, New York, New York 10021, USA
³ National Magnetic Resonance Facility at Madison, Department of Biochemistry, University of Wisconsin–Madison, Madison, Wisconsin 35705, USA
⁴ Institute of Computational Chemistry and Department of Chemistry, University of Girona, 17071 Girona (Catalonia), Spain
⁵ Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic and Foundation, Rochester, Minnesota, 55905 USA

(RECEIVED November 2, 2007; FINAL REVISION December 26, 2007; ACCEPTED December 27, 2007)

Protein folding can introduce strain in peptide covalent geometry, including deviations from planarity that are difficult to detect, especially for a protein in solution. We have found dependencies in protein backbone ² J _NC' couplings on the planarity and the relative orientation of the sequential peptide planes. These dependences were observed in experimental ² J _NC' couplings from seven proteins, and also were supported by DFT calculations for a model tripeptide. Findings indicate that elevated ² J _NC' couplings may serve as reporters of structural strain in the protein backbone imposed by protein folds. Such information, supplemented with the H-bond strengths derived from ^h3 J _NC' couplings, provides useful insight into the overall energy profile of the protein backbone in solution.

Keywords: DFT; H-bond; 2JNC' scalar coupling; NMR; protein structure

Supplemental material: see www.proteinscience.org

Reprint requests to: Nenad Jurani, Mayo Foundation, 200 First Street Southwest, Rochester, MN 55905, USA; e-mail: juranic.nenad{at}mayo.edu; fax: (507) 284-8433; or J.J. Dannenberg, Department of Chemistry, City University of New York, Hunter College and the Graduate School, 695 Park Avenue, New York, NY 10021, USA; e-mail: jdannenberg{at}gc.cuny.edu; fax: (212) 772-5332.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.073331608.

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