Self-consistent 3J coupling analysis for the joint calibration of Karplus coefficients and evaluation of torsion angles.
作者： Jürgen M. Schmidt , Markus Blümel , Frank Löhr , Heinz Rüterjans
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摘要: The concept of self-consistent J coupling evaluation exploits redundant structure information inherent in large sets 3J constants. Application to the protein Desulfovibrio vulgaris flavodoxin demonstrates simultaneous refinement torsion-angle values and related Karplus coefficients. experimental basis includes quantitative constants polypeptide backbone φ torsion originating from a variety heteronuclear 2D 3D NMR correlation experiments, totalling 124 3J(HN,Hα), 129 3J(HN,C′), 121 3J(HN,Cβ), 128 3J(C′i−1,Hαi), 3J(C′i−1,C′i), 122 3J(C′i−1,Cβi). Without prior knowledge either X-ray crystallography or data, such as NOE distance constraints, accurate dihedral angles are specified for non-glycine non-proline residues out total 147 amino acids. Different models molecular internal mobility considered. coefficients obtained applicable conformational analysis torsions other polypeptides.
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