Biological Nmr Part A
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| Author | : John L. Markley |
| Publisher | : Oxford University Press |
| Total Pages | : 375 |
| Release | : 1997-01-30 |
| Genre | : Medical |
| ISBN | : 0195094689 |
This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications. The book, in honor of Oleg Jardetsky, one of the pioneers of the field, is edited by two of the most highly respected investigators using NMR, and features contributions by most of the leading workers in the field. It will be valued as a landmark publication that presents the state-of-the-art perspectives regarding one of today's most important technologies.
| Author | : Michaeleen Doucleff |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 166 |
| Release | : 2011-01-03 |
| Genre | : Science |
| ISBN | : 3642162517 |
Steering clear of quantum mechanics and product operators, "Pocket Guide to Biomolecular NMR" uses intuitive, concrete analogies to explain the theory required to understand NMR studies on the structure and dynamics of biological macromolecules. For example, instead of explaining nuclear spin with angular momentum equations or Hamiltonians, the books describes nuclei as "bells" in a choir, ringing at specific frequencies depending on the atom type and their surrounding electromagnetic environment.This simple bell analogy, which is employed throughout the book, has never been used to explain NMR and makes it surprisingly easy to learn complex, bewildering NMR concepts, such as dipole-dipole coupling and CPMG pulse sequences. Other topics covered include the basics of multi-dimensional NMR, relaxation theory, and Model Free analysis. The small size and fast pace of “Pocket Guide to Biomolecular NMR” makes the book a perfect companion to traditional biophysics and biochemistry textbooks, but the book's unique perspective will provide even seasoned spectroscopists with new insights and handy “thought” short-cuts.
| Author | : A.Joshua Wand |
| Publisher | : Academic Press |
| Total Pages | : 442 |
| Release | : 2019-01-03 |
| Genre | : Science |
| ISBN | : 0128138610 |
Biological NMR, Part A, the latest release in the Methods of Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters on topics such as Protein methyl labeling, Membrane protein expression – yeast, Protein aromatic labeling, His-tag/Metal contamination, Bicelles, nanodiscs and micelles MP host, PTM – phosphorylation, PTM – lipidation, Screening platform for receptor-ligand discovery Solution Spectroscopy, Large protein strategies, NUS data collection/analysis, F19 incl. hydration, ODNP - hydration, Reverse micelle - Hydration Solid State Spectroscopy, SS NMR membrane proteins, SS NMR soluble/aggregate proteins, SS DNP - general, SS NMR nucleic acids, Structure determination and computer analysis, and much more. - Provides the authority and expertise of leading contributors from an international board of authors - Presents the latest release in the Methods of Enzymology series - Updated release includes the latest information on the Biological NMR
| Author | : Jeremy N. S. Evans |
| Publisher | : Oxford University Press, USA |
| Total Pages | : 444 |
| Release | : 1995 |
| Genre | : Science |
| ISBN | : 9780198547662 |
The technique of nuclear magnetic resonance (NMR) spectroscopy is an important tool in biochemistry and biophysics for the understanding of the structure and ultimately, the function of biomolecules. This textbook explains the salient features of biological NMR spectroscopy to undergraduates and postgraduates taking courses in NMR, biological NMR, physical biochemistry, and biophysics. Unlike other books in the general field of NMR (except the advanced treatises), the approach here is tointroduce and make use of quantum mechanical product operators as well as the classical vector method of explaining the bewildering array of pulse sequences available today. The book covers two- dimensional, three- dimensional, and four- dimensional NMR and their application to protein and DNA structure determination. A unique feature is the coverage of the biological aspects of solid- state NMR spectroscopy. The author provides many selected examples from the research literature, illustratingthe applications of NMR spectroscopy to biological proteins.
| Author | : Gordon S. Rule |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 543 |
| Release | : 2006-02-16 |
| Genre | : Science |
| ISBN | : 1402035004 |
NMR spectroscopy has proven to be a powerful technique to study the structure and dynamics of biological macromolecules. Fundamentals of Protein NMR Spectroscopy is a comprehensive textbook that guides the reader from a basic understanding of the phenomenological properties of magnetic resonance to the application and interpretation of modern multi-dimensional NMR experiments on 15N/13C-labeled proteins. Beginning with elementary quantum mechanics, a set of practical rules is presented and used to describe many commonly employed multi-dimensional, multi-nuclear NMR pulse sequences. A modular analysis of NMR pulse sequence building blocks also provides a basis for understanding and developing novel pulse programs. This text not only covers topics from chemical shift assignment to protein structure refinement, as well as the analysis of protein dynamics and chemical kinetics, but also provides a practical guide to many aspects of modern spectrometer hardware, sample preparation, experimental set-up, and data processing. End of chapter exercises are included to emphasize important concepts. Fundamentals of Protein NMR Spectroscopy not only offer students a systematic, in-depth, understanding of modern NMR spectroscopy and its application to biomolecular systems, but will also be a useful reference for the experienced investigator.
| Author | : John Cavanagh |
| Publisher | : Elsevier |
| Total Pages | : 915 |
| Release | : 2010-07-21 |
| Genre | : Science |
| ISBN | : 008047103X |
Protein NMR Spectroscopy, Second Edition combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, the book develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments. Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. This updated version includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced. The book is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or wish to understand the latest developments in this field. - Provides an understanding of the theoretical principles important for biological NMR spectroscopy - Demonstrates how to implement, optimize and troubleshoot modern multi-dimensional NMR experiments - Allows for the capability of designing effective experimental protocols for investigations of protein structures and dynamics - Includes a comprehensive set of example NMR spectra of ubiquitin provides a reference for validation of experimental methods
| Author | : K.V.R. Chary |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 552 |
| Release | : 2008-04-01 |
| Genre | : Science |
| ISBN | : 1402066805 |
During teaching NMR to students and researchers, we felt the need for a text-book which can cover modern trends in the application of NMR to biological systems. This book covers the entire area of NMR in Biological Sciences (Biomolecules, cells and tissues, animals, plants and drug design). As well as being useful to researchers, this is an excellent book for teaching a course on NMR in Biological Systems.
| Author | : Thomas C. Pochapsky |
| Publisher | : Garland Science |
| Total Pages | : 395 |
| Release | : 2006-06-30 |
| Genre | : Science |
| ISBN | : 1136843728 |
Nuclear Magnetic Resonance spectroscopy is a dynamic way for scientists of all kinds to investigate the physical, chemical, and biological properties of matter. Its many applications make it a versatile tool previously subject to monolithic treatment in reference-style texts. Based on a course taught for over ten years at Brandeis University, this is the first textbook on NMR spectroscopy for a one-semester course or self-instruction. In keeping with the authors' efforts to make it a useful textbook, they have included problems at the end of each chapter. The book not only covers the latest developments in the field, such as GOESY (Gradient Enhanced Overhauser Spectroscopy) and multidimensional NMR, but includes practical examples using real spectra and associated problem sets. Assuming the reader has a background of chemistry, physics and calculus, this textbook will be ideal for graduate students in chemistry and biochemistry, as well as biology, physics, and biophysics. NMR for Physical and Biological Scientists will also be useful to medical schools, research facilities, and the many chemical, pharmaceutical, and biotech firms that offer in-house instruction on NMR spectroscopy.
| Author | : A. Kristina Downing |
| Publisher | : Humana |
| Total Pages | : 487 |
| Release | : 2004-08-17 |
| Genre | : Science |
| ISBN | : 9781588292469 |
When I was asked to edit the second edition of Protein NMR Techniques, my first thought was that the time was ripe for a new edition. The past several years have seen a surge in the development of novel methods that are truly revolutionizing our ability to characterize biological macromolecules in terms of speed, accuracy, and size limitations. I was particularly excited at the prospect of making these techniques accessible to all NMR labs and for the opportunity to ask the experts to divulge their hints and tips and to write, practically, about the methods. I commissioned 19 chapters with wide scope for Protein NMR Techniques, and the volume has been organized with numerous themes in mind. Chapters 1 and 2 deal with recombinant protein expression using two organisms, E. coli and P. pastoris, that can produce high yields of isotopically labeled protein at a reasonable cost. Staying with the idea of isotopic labeling, Chapter 3 describes methods for perdeuteration and site-specific protonation and is the first of several chapters in the book that is relevant to studies of higher molecular weight systems. A different, but equally powerful, method that uses molecular biology to “edit” the spectrum of a large molecule using segmental labeling is presented in Chapter 4. Having successfully produced a high molecular weight target for study, the next logical step is data acquisition. Hence, the final chapter on this theme, Chapter 5, describes TROSY methods for stru- ural studies.
| Author | : Andrew J. Dingley |
| Publisher | : IOS Press |
| Total Pages | : 488 |
| Release | : 2011 |
| Genre | : Medical |
| ISBN | : 1607506947 |
Nuclear Magnetic Resonance (NMR) spectroscopy is the most powerful technique for characterization of biomolecular structures at atomic resolution in the solution state. This timely book, entitled "Biomolecular NMR Spectroscopy," focuses on the latest state-of-the-art NMR techniques for characterization of biological macromolecules in the solid and solution state. The editors, Dr. Andrew Dingley (University of Auckland, New Zealand) and Dr. Steven Pascal (Massey University, New Zealand) have organized the book into four sections, covering the following topics: sample preparation, structure and dynamics of proteins, structure and dynamics of nucleic acids and protein-nucleic acid complexes, and rapid and hybrid techniques--
