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Protein Nmr Spectroscopy

Author: Gordon Roberts
Publisher: John Wiley & Sons
ISBN: 1119972825
Size: 61.46 MB
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Nuclear Magnetic Resonance (NMR) spectroscopy, a physical phenomenon based upon the magnetic properties of certain atomic nuclei, has found a wide range of applications in life sciences over recent decades. The dramatic advances in NMR techniques have led to corresponding advances in the ability of NMR to study structure, dynamics and interactions of biological macromolecules in solution under close to physiological conditions. This volume focuses on the use of NMR to study proteins. NMR can be used to determine detailed three-dimensional structures of proteins in solution. Furthermore, it provides information about conformational or chemical exchange, internal mobility and dynamics at timescales varying from pcoseconds to seconds. It is the primary technique used to obtain information on intrinsically disordered (unfolded) proteins, since these proteins will not crystallize easily. NMR is also a very powerful method for the study of interactions of protein with other molecules, whether small molecules (including drugs), nuclear acids or other proteins. This up-to-date volume covers NMR techiniques and their application to proteins, with a focus on practical details. This book will provide a newcomer to NMR with the practical guidance in order to carry out successful experiments with proteins and to analyze the resulting spectra. Those who are familiar with the chemical applications of NMR will also find is useful in understanding the special requirements of protien NMR.

Protein Nmr Spectroscopy

Author: Lu-Yun Lian
Publisher: John Wiley & Sons
ISBN: 0470721936
Size: 43.60 MB
Format: PDF, ePub, Mobi
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Nuclear Magnetic Resonance (NMR) spectroscopy, a physical phenomenon based upon the magnetic properties of certain atomic nuclei, has found a wide range of applications in life sciences over recent decades. This up-to-date volume covers NMR techniques and their application to proteins, with a focus on practical details. Providing newcomers to NMR with practical guidance to carry out successful experiments with proteins and analyze the resulting spectra, those familiar with the chemical applications of NMR will also find it useful in understanding the special requirements of protein NMR.

Protein Nmr Spectroscopy

Author: John Cavanagh
Publisher: Academic Press
ISBN: 9780121644901
Size: 12.34 MB
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Protein NMR Spectroscopy: Principles and Practice combines a comprehensive theoretical treatment of high resolution NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy: Principles and Practice develops the complete repertoire of theoretical principals and experimental practices necessary for understanding and implementing the most sophisticated NMR experiments. Protein NMR Spectroscopy: Principles and Practice is written as a graduate-level textbook and will be of particular interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy as a research tool or who wish to remain abreast of the latest developments in this increasingly important area. * Special Features: * First book to combine detailed NMR theory discussions with experimental applications to biomolecules. * All the theory required to understand these experiments and others. * Easy to follow progression from a fundamental level to an advanced level. * Theory of NMR and practical applications for biomolecular investigations presented. * Theory applied to very practical situations. * Comprehensive treatment of different "levels" of theory from simple ideas to density matrix analysis and operator practices. * Comprehensive description of multi dimensional NMR experiments as applied to unlabeled, 15N-labeled and doubly (13C/15N) labeled proteins.

Fundamentals Of Protein Nmr Spectroscopy

Author: Gordon S. Rule
Publisher: Springer Science & Business Media
ISBN: 1402035004
Size: 21.30 MB
Format: PDF
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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.

Applications Of Nmr Spectroscopy

Author: Atta-ur-Rahman
Publisher: Elsevier
ISBN: 1608059650
Size: 55.41 MB
Format: PDF, ePub
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Applications of NMR Spectroscopy, Volume 2, originally published by Bentham and now distributed by Elsevier, presents the latest developments in the field of NMR spectroscopy, including the analysis of plant polyphenols, the role of NMR spectroscopy in neuroradiology, NMR-based sensors, studies on protein and nucleic acid structure and function, and mathematical formations for NMR spectroscopy in structural biology. The fully illustrated chapters contain comprehensive references to the recent literature. The applications presented cover a wide range of the field, such as drug development, medical imaging and diagnostics, food science, mining, petrochemical, process control, materials science, and chemical engineering, making this resource a multi-disciplinary reference with broad applications. The content is ideal for readers who are seeking reviews and updates, as it consolidates scientific articles of a diverse nature into a single volume. Sections are organized based on disciplines, such as food science and medical diagnostics. Each chapter is written by eminent experts in the field. Consolidates the latest developments in NMR spectroscopy into a single volume Authored and edited by world-leading experts in spectroscopy Features comprehensive references to the most recent related literature More than 65 illustrations aid in the retention of key concepts

High Resolution Nmr Techniques In Organic Chemistry

Author: Timothy D. W. Claridge
Publisher: Elsevier
ISBN: 9780080427997
Size: 39.93 MB
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From the initial observation of proton magnetic resonance in water and in paraffin, the discipline of nuclear magnetic resonance has seen unparalleled growth as an analytical method. Modern NMR spectroscopy is a highly developed, yet still evolving, subject which finds application in chemistry, biology, medicine, materials science and geology. In this book, emphasis is on the more recently developed methods of solution-state NMR applicable to chemical research, which are chosen for their wide applicability and robustness. These have, in many cases, already become established techniques in NMR laboratories, in both academic and industrial establishments. A considerable amount of information and guidance is given on the implementation and execution of the techniques described in this book.

Protein Nuclear Magnetic Resonance Techniques

Author: Anna Kristina Downing
Publisher: Springer Science & Business Media
ISBN: 1592598099
Size: 16.67 MB
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This second edition of Protein NMR Techniques is well written with a dynamic approach that covers multiple topics within its nineteen chapters. The text opens with a review of recombinant protein expression using two organisms, E. coli and P. pastoris that can produce high yields of isotopically labeled protein at a reasonable cost. The focus then shifts slightly to studies of aligned molecules, starting with a chapter on different options for the preparation of an aligned sample. The text also provides a comprehensive review of the use of RDCs to the study protein dynamics highlights and the range of information accessible using these methods. The book concludes with a concise explanation of the application of solid-state methods and the study of membrane proteins, a particularly important but difficult class of targets.

Structural Biology

Author: Quincy Teng
Publisher: Springer Science & Business Media
ISBN: 1461439647
Size: 27.48 MB
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This 2nd edition begins with an overview of NMR development and applications in biological systems. It describes recent developments in instrument hardware and methodology. Chapters highlight the scope and limitation of NMR methods. While detailed math and quantum mechanics dealing with NMR theory have been addressed in several well-known NMR volumes, chapter two of this volume illustrates the fundamental principles and concepts of NMR spectroscopy in a more descriptive manner. Topics such as instrument setup, data acquisition, and data processing using a variety of offline software are discussed. Chapters further discuss several routine stategies for preparing samples, especially for macromolecules and complexes. The target market for such a volume includes researchers in the field of biochemistry, chemistry, structural biology and biophysics.

Nmr Spectroscopy

Author: Harald Günther
Publisher: John Wiley & Sons
ISBN: 3527674772
Size: 34.87 MB
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Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful and widely used techniques in chemical research for investigating structures and dynamics of molecules. Advanced methods can even be utilized for structure determinations of biopolymers, for example proteins or nucleic acids. NMR is also used in medicine for magnetic resonance imaging (MRI). The method is based on spectral lines of different atomic nuclei that are excited when a strong magnetic field and a radiofrequency transmitter are applied. The method is very sensitive to the features of molecular structure because also the neighboring atoms influence the signals from individual nuclei and this is important for determining the 3D-structure of molecules. This new edition of the popular classic has a clear style and a highly practical, mostly non-mathematical approach. Many examples are taken from organic and organometallic chemistry, making this book an invaluable guide to undergraduate and graduate students of organic chemistry, biochemistry, spectroscopy or physical chemistry, and to researchers using this well-established and extremely important technique. Problems and solutions are included.

Applied Nmr Spectroscopy For Chemists And Life Scientists

Author: Oliver Zerbe
Publisher: John Wiley & Sons
ISBN: 3527677836
Size: 45.44 MB
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From complex structure elucidation to biomolecular interactions - this applicationoriented textbook covers both theory and practice of modern NMR applications. Part one sets the stage with a general description of NMR introducing important parameters such as the chemical shift and scalar or dipolar couplings. Part two describes the theory behind NMR, providing a profound understanding of the involved spin physics, deliberately kept shorter than in other NMR textbooks, and without a rigorous mathematical treatment of all the physico-chemical computations. Part three discusses technical and practical aspects of how to use NMR. Important phenomena such as relaxation, exchange, or the nuclear Overhauser effects and the methods of modern NMR spectroscopy including multidimensional experiments, solid state NMR, and the measurement of molecular interactions are the subject of part four. The final part explains the use of NMR for the structure determination of selected classes of complex biomolecules, from steroids to peptides or proteins, nucleic acids, and carbohydrates. For chemists as well as users of NMR technology in the biological sciences.