Modern Techniques in Protein NMR
N. Rama Krishna, Lawrence Berliner
Springer US, Apr 30, 1999 - Medical - 387 pages
Volume 16 marks the beginning of a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series. This volume is being followed by Volume 17 with the subtitle Structure Computation and Dynamics in Protein NMR. Volumes 16 and 17 present some of the recent, significant advances in biomolecular NMR field with emphasis on developments during the last five years. We are honored to have brought together in these volumes some of the world’s foremost experts who have provided broad leadership in advancing this field. Volume 16 contains advances in two broad categories: the first, Large Proteins, Complexes, and Membrane Proteins, and second, Pulse Methods. Volume 17, which will follow covers major advances in Computational Methods, and Structure and Dynamics. In the opening chapter of Volume 16, Marius Clore and Angela Gronenborn give a brief review of NMR strategies including the use of long range restraints in the structure determination of large proteins and protein complexes. In the next two chapters, Lewis Kay and Ron Venters and their collaborators describe state-of-t- art advances in the study of perdeuterated large proteins. They are followed by Stanley Opella and co-workers who present recent developments in the study of membrane proteins. (A related topic dealing with magnetic field induced residual dipolar couplings in proteins will appear in the section on Structure and Dynamics in Volume 17).
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Determining Structures of Large Proteins and Protein
within a Protein
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aliphatic amide protons amino acids applied bilayers Biochemistry Biol Biomol calculated calmodulin Chem chemical shift chemical-shift Clore coherence coli complex constant-time correlation coupling constants cross-correlated cross-correlated relaxation cross-peak decoupling deuterium dihedral angle dipolar coupling distance restraints E.COSY etal experimental Fesik Figure fractional deuteration frequency fully protonated Gardner Gronenborn Grzesiek heteronuclear highly deuterated proteins HNCA HNCACB homonuclear HSQC Hu and Bax interaction intraresidue isotopomers LeMaster linewidths Magn measured membrane proteins methods methyl groups Metzler micelles molecular molecules Muhandiram multiplet NMR spectroscopy NOESY NOESY experiments nuclei observed obtained Opella oriented peak peptide perdeuterated protein PLCC Protein NMR protons pulse sequence relaxation rates residues sample scalar coupling secondary structure sensitivity sequential SH2 domain shown in Fig sidechain solid-state NMR solution NMR spectra spectrum spin systems structure determination T2 relaxation tensor torsion angle triple-resonance uniformly 15N labeled values Vuister Yamazaki