caa a22 4500 477136370 CHVBK 20180405111719.0 cr unu---uuuuu 170330e19970401xx s 000 0 eng 10.1023/A:1018631009583 doi (NATIONALLICENCE)springer-10.1023/A:1018631009583 Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13Cα nuclear spin relaxation [Elektronische Daten] [Larry Lee, Mark Rance, Walter Chazin, Arthur Palmer III] Current methods of determining the rotational diffusion tensors of proteins in solution byNMR spectroscopy exclusively utilize relaxation rate constants for backbone amide 15N spins.However, the distributions of orientations of N-H bond vectors are not isotropic in manyproteins, and correlations between bond vector orientations reduce the accuracy and precisionof rotational diffusion tensors extracted from 15N spin relaxation data. The inclusion of both13Cα and 15N spin relaxation rate constants increases the robustness of the diffusiontensor analysis because the orientations of the Cα-Hα bond vectors differ from theorientations of the N-H bond vectors. Theoretical and experimental results for calbindin D9k,granulocyte colony stimulating factor, and ubiquitin, three proteins with different distributionsof N-H and Cα-Hα bond vectors, are used to illustrate the advantages of thesimultaneous utilization of 13Cα and 15N relaxation data. Kluwer Academic Publishers, 1997 Proteins nationallicence Nuclear spin relaxation nationallicence Rotational diffusion tensor anisotropy nationallicence Lee Larry Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, 10032, New York, NY, U.S.A aut Rance Mark Department of Molecular Genetics, Biochemistry, and Molecular Biology, University of Cincinnati, 45267, Cincinnati, OH, U.S.A aut Chazin Walter Department of Molecular Biology, The Scripps Research Institute, 10666 North Torrey Pines Road, 92037, La Jolla, CA, U.S.A aut Palmer III Arthur Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, 10032, New York, NY, U.S.A aut Journal of Biomolecular NMR Kluwer Academic Publishers 9/3(1997-04-01), 287-298 0925-2738 9:3<287 1997 9 10858 https://doi.org/10.1023/A:1018631009583 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018631009583 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lee Larry Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, 10032, New York, NY, U.S.A aut NATIONALLICENCE 700 1- Rance Mark Department of Molecular Genetics, Biochemistry, and Molecular Biology, University of Cincinnati, 45267, Cincinnati, OH, U.S.A aut NATIONALLICENCE 700 1- Chazin Walter Department of Molecular Biology, The Scripps Research Institute, 10666 North Torrey Pines Road, 92037, La Jolla, CA, U.S.A aut NATIONALLICENCE 700 1- Palmer III Arthur Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, 10032, New York, NY, U.S.A aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 9/3(1997-04-01), 287-298 0925-2738 9:3<287 1997 9 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer