Juranic, Nenad Dannenberg, J. J. Cornilescu, Gabriel Salvador, Pedro Atanasova, Elena Ahn, Hee-Chul Macura, Slobodan Markley, John L. Prendergast, Franklyn G. 2024-01-20T23:33:00Z 2024-01-20T23:33:00Z 2021-08-31 2008-04 0961-8368 https://pubs.kist.re.kr/handle/201004/133624 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. English WILEY-BLACKWELL DENSITY-FUNCTIONAL THEORY NUCLEAR-MAGNETIC-RESONANCE BOND C-13-N-15 3-BOND CALCIUM-FREE CALMODULIN BASIS-SET DEPENDENCE N-15 NMR RELAXATION SCALAR J-COUPLINGS HYDROGEN-BONDS HIGH-RESOLUTION HUMAN UBIQUITIN Structural dependencies of protein backbone (2)J(NC') couplings Article 10.1110/ps.073331608 1 PROTEIN SCIENCE, v.17, no.4, pp.768 - 776 PROTEIN SCIENCE 17 4 768 776 scie scopus 000254197800018 2-s2.0-41649118825 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article DENSITY-FUNCTIONAL THEORY NUCLEAR-MAGNETIC-RESONANCE BOND C-13-N-15 3-BOND CALCIUM-FREE CALMODULIN BASIS-SET DEPENDENCE N-15 NMR RELAXATION SCALAR J-COUPLINGS HYDROGEN-BONDS HIGH-RESOLUTION HUMAN UBIQUITIN DFT H-bond 2JNC&apos scalar coupling NMR protein structure