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Structural dependencies of protein backbone 2 J NC′ couplings
Author(s) -
Juranić Nenad,
Dannenberg J.J.,
Cornilescu Gabriel,
Salvador Pedro,
Atanasova Elena,
Ahn HeeChul,
Macura Slobodan,
Markley John L.,
Prendergast Franklyn G.
Publication year - 2008
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.073331608
Subject(s) - planarity testing , tripeptide , crystallography , peptide , covalent bond , chemistry , protein folding , folding (dsp implementation) , peptide bond , protein structure , chemical physics , computational chemistry , physics , biochemistry , organic chemistry , electrical engineering , engineering
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.