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Protein Nmr Spectroscopy

Author: Gordon Roberts
Publisher: John Wiley & Sons
ISBN: 1119972825
Size: 79.72 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: 63.24 MB
Format: PDF, Kindle
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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: Elsevier
ISBN: 9780080471037
Size: 75.62 MB
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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

Fundamentals Of Protein Nmr Spectroscopy

Author: Gordon S. Rule
Publisher: Springer Science & Business Media
ISBN: 1402035004
Size: 34.58 MB
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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: Bentham Science Publishers
ISBN: 1681081431
Size: 56.71 MB
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Applications of NMR Spectroscopy is a book series devoted to publishing the latest advances in the applications of nuclear magnetic resonance (NMR) spectroscopy in various fields of organic chemistry, biochemistry, health and agriculture. The fourth volume of the series features several reviews focusing on NMR spectroscopic techniques in food sciences. Readers will find references on methods used to test food quality, food color analysis, the role of Tannins in wine taste as well as NMR studies on lipid oxidation and large protein complexes.

Structural Biology

Author: Quincy Teng
Publisher: Springer Science & Business Media
ISBN: 1461439647
Size: 56.97 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.

Protein Nuclear Magnetic Resonance Techniques

Author: Anna Kristina Downing
Publisher: Springer Science & Business Media
ISBN: 1592598099
Size: 33.77 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.

Nmr Spectroscopy

Author: Harald Günther
Publisher: John Wiley & Sons
ISBN: 3527674772
Size: 15.60 MB
Format: PDF
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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.

High Resolution Nmr Techniques In Organic Chemistry

Author: Timothy D. W. Claridge
Publisher: Newnes
ISBN: 0080546285
Size: 11.10 MB
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"Nuclear Magnetic Resonance (NMR) Spectroscopy remains the foremost analytical technique for the structure elucidation of organic molecules and an indispensable tool for the synthetic, medicinal and natural product chemist. New techniques continue to emerge and the application of NMR methods continues to expand. High-Resolution NMR Techniques in Organic Chemistry is designed for use in academic and industrial NMR facilities, as a text for graduate-level NMR courses, and as an accessible reference for the chemist's or spectroscopist's desk." --Book Jacket.

Understanding Nmr Spectroscopy

Author: James Keeler
Publisher: John Wiley & Sons
ISBN: 1119964938
Size: 55.85 MB
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This text is aimed at people who have some familiarity with high-resolution NMR and who wish to deepen their understanding of how NMR experiments actually ‘work’. This revised and updated edition takes the same approach as the highly-acclaimed first edition. The text concentrates on the description of commonly-used experiments and explains in detail the theory behind how such experiments work. The quantum mechanical tools needed to analyse pulse sequences are introduced set by step, but the approach is relatively informal with the emphasis on obtaining a good understanding of how the experiments actually work. The use of two-colour printing and a new larger format improves the readability of the text. In addition, a number of new topics have been introduced: How product operators can be extended to describe experiments in AX2 and AX3 spin systems, thus making it possible to discuss the important APT, INEPT and DEPT experiments often used in carbon-13 NMR. Spin system analysis i.e. how shifts and couplings can be extracted from strongly-coupled (second-order) spectra. How the presence of chemically equivalent spins leads to spectral features which are somewhat unusual and possibly misleading, even at high magnetic fields. A discussion of chemical exchange effects has been introduced in order to help with the explanation of transverse relaxation. The double-quantum spectroscopy of a three-spin system is now considered in more detail. Reviews of the First Edition “For anyone wishing to know what really goes on in their NMR experiments, I would highly recommend this book” – Chemistry World “…I warmly recommend for budding NMR spectroscopists, or others who wish to deepen their understanding of elementary NMR theory or theoretical tools” – Magnetic Resonance in Chemistry