Biological Magnetic Resonance - Volume 16: Modern Techniques in Protein NMR (Biological Magnetic Resonance)

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). Annotation. Describes techniques and applications that have emerged since the previous volume in the series on spin labeling in 1989, and marks a shift in the series to topic-focused volumes. Among the topics are the analysis of spin-label line shapes with novel inhomogeneous broadening from different components widths and applications to spatially disconnected domains in membranes, a comparison of spin-label spectra at X-band and W-band, the site- directed spin labeling of membrane proteins and of interactions between peptides and membranes, spin-labeled nucleic acids, and electron paramagnetic resonance studies of living animals and related model systems. Annotation copyrighted by Book News, Inc., Portland, OR Front Matter....Pages 1-1 Determining Structures of Large Proteins and Protein Complexes by NMR....Pages 3-26 Multidimensional 2 H-Based NMR Methods for Resonance Assignment, Structure Determination, and The Study of Protein Dynamics....Pages 27-74 NMR of Perdeuterated Large Proteins....Pages 75-120 Recent Developments in Multidimensional NMR Methods for Structural Studies of Membrane Proteins....Pages 121-145 Front Matter....Pages 147-147 Homonuclear Decoupling in Proteins....Pages 149-193 Pulse Sequences for Measuring Coupling Constants....Pages 195-257 Methods for the Determination of Torsion Angle Restraints in Biomacromolecules....Pages 259-367 [This] volume ... represents significant advances in the biomolecular NMR field, with emphasis on developments during the recent years. This book brings together some of the world's foremost experts who have provided broad leadership in advancing the field. [It] is devoted to topics on biomacromolecules and pulse methods. It covers advances in the study of large proteins and protein complexes, methods involving perdeuterated large proteins, membrane proteins, advances in pulse schemes for spin decoupling and for the measurement of coupling constants and torsion angle constraints including cross-correlated relaxation spectroscopy Biological Magnetic Resonance represents significant advances in the biomolecular NMR field, with emphasis on developments during the last five years. This book brings together some of the world's foremost experts who have provided broad leadership in advancing the field. Volume 16 is devoted to topics on biomacromolecules and pulse methods. This volume covers important advances in the study of large proteins and protein complexes, methods involving perdeuterated large proteins, membrane proteins, advances in pulse schemes for spin decoupling and for the measurement of coupling constants and torsion angle constraints. Thanks to the vast progress made in the investigation of biomolecules using NMR over the last few years, NMR spectroscopy offers a universal tool for examining the binding of an active substance to its target protein. Its use thereby benefits the rational development of drugs. This interaction can now be investigated in a hitherto unparalleled precision and displayed in 3D - an important prerequisite for the targeted development of new active substances. Thus it comes as no surprise that a large number of the authors are working for leading pharmaceutical companies. The book presents the theor