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Protein Nmr Spectroscopy

Author: Gordon Roberts
Publisher: John Wiley & Sons
ISBN: 1119972825
Size: 76.15 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: John Cavanagh
Publisher: Elsevier
ISBN: 9780080471037
Size: 54.79 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

Protein Nmr

Author: Lawrence Berliner
Publisher: Springer
ISBN: 1489976213
Size: 39.87 MB
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This book covers new techniques in protein NMR, from basic principles to state-of-the-art research. It covers a spectrum of topics ranging from a “toolbox” for how sequence-specific resonance assignments can be obtained using a suite of 2D and 3D NMR experiments and tips on how overlap problems can be overcome. Further topics include the novel applications of Overhauser dynamic nuclear polarization methods (DNP), assessing protein structure, and aspects of solid-state NMR of macroscopically aligned membrane proteins. This book is an ideal resource for students and researchers in the fields of biochemistry, chemistry, and pharmacology and NMR physics. Comprehensive and intuitively structured, this book examines protein NMR and new novel applications that include the latest technological advances. This book also has the features of: • A selection of various applications and cutting-edge advances, such as novel applications of Overhauser dynamic nuclear polarization methods (DNP) and a suite of 2D and 3D NMR experiments and tips on how overlap problems can be overcome • A pedagogical approach to the methodology • Engaging the reader and student with a clear, yet critical presentation of the applications

Nuclear Magnetic Resonance

Author:
Publisher: Royal Society of Chemistry
ISBN: 1849738122
Size: 63.83 MB
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Now in its 43rd volume, the Specialist Periodical Report in Nuclear Magnetic Resonance presents comprehensive and critical reviews of the recent literature, providing the reader with an informed summary of the field from invited authors. Several chapters in this volume are devoted to biochemistry, focussing on carbohydrates, lipids, and proteins and nucleic acids; Malcolm Prior also presents a chapter examining the recent literature of NMR in living systems and Cynthia Jameson reviews the theoretical and physical aspects of nuclear shielding, while Jaroslaw Jazwinski examines the theoretical aspects of spin-spin couplings. The lead volume editor, Krystyna Kamienska-Trela, presents a chapter on the applications of spin-spin couplings. Anyone wishing to update themselves on the recent and hottest developments in NMR will benefit from this volume, which deserves a place in any library or NMR facility. Purchasers of the print edition can register for free access to the electronic edition by returning the enclosed registration card.

Methods In Molecular Biophysics

Author: Nathan R. Zaccai
Publisher: Cambridge University Press
ISBN: 1108508804
Size: 62.40 MB
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Current techniques for studying biological macromolecules and their interactions are based on the application of physical methods, ranging from classical thermodynamics to more recently developed techniques for the detection and manipulation of single molecules. Reflecting the advances made in biophysics research over the past decade, and now including a new section on medical imaging, this new edition describes the physical methods used in modern biology. All key techniques are covered, including mass spectrometry, hydrodynamics, microscopy and imaging, diffraction and spectroscopy, electron microscopy, molecular dynamics simulations and nuclear magnetic resonance. Each method is explained in detail using examples of real-world applications. Short asides are provided throughout to ensure that explanations are accessible to life scientists, physicists and those with medical backgrounds. The book remains an unparalleled and comprehensive resource for graduate students of biophysics and medical physics in science and medical schools, as well as for research scientists looking for an introduction to techniques from across this interdisciplinary field.

Fundamentals Of Protein Nmr Spectroscopy

Author: Gordon S. Rule
Publisher: Springer Science & Business Media
ISBN: 1402035004
Size: 53.84 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.

High Resolution Nmr Techniques In Organic Chemistry

Author: Timothy D.W. Claridge
Publisher: Elsevier
ISBN: 008099993X
Size: 36.38 MB
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High-Resolution NMR Techniques in Organic Chemistry, Third Edition describes the most important NMR spectroscopy techniques for the structure elucidation of organic molecules and the investigation of their behaviour in solution. Appropriate for advanced undergraduate and graduate students, research chemists and NMR facility managers, this thorough revision covers practical aspects of NMR techniques and instrumentation, data collection, and spectrum interpretation. It describes all major classes of one- and two-dimensional NMR experiments including homonuclear and heteronuclear correlations, the nuclear Overhauser effect, diffusion measurements, and techniques for studying protein–ligand interactions. A trusted authority on this critical expertise, High-Resolution NMR Techniques in Organic Chemistry, Third Edition is an essential resource for every chemist and NMR spectroscopist.

Nmr Spectroscopy

Author: Harald Günther
Publisher: John Wiley & Sons
ISBN: 3527674772
Size: 60.83 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.

Protein Nuclear Magnetic Resonance Techniques

Author: Anna Kristina Downing
Publisher: Springer Science & Business Media
ISBN: 1592598099
Size: 44.50 MB
Format: PDF
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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 Of Biological Solids

Author: A. Ramamoorthy
Publisher: CRC Press
ISBN: 1420027611
Size: 59.36 MB
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Over the past decade, a myriad of techniques have shown that solid-state nuclear magnetic resonance (NMR) can be used in a broad spectrum of applications with exceptionally impressive results. Solid-state NMR results can yield high-resolution details on the structure and function of many important biological solids, including viruses, fibril-forming molecules, and molecules embedded in the cell membrane. Filling a void in the current literature, NMR Spectroscopy of Biological Solids examines all the recent developments, implementation, and interpretation of solid-state NMR experiments and the advantages of applying them to biological systems. The book emphasizes how these techniques can be used to realize the structure of non-crystalline systems of any size. It explains how these isotropic and anisotropic couplings interactions are used to determine atomic-level structures of biological molecules in a non-soluble state and extrapolate the three-dimensional structure of membrane proteins using magic-angle spinning (MAS). The book also focuses on the use of multidimensional solid-state NMR methods in the study of aligned systems to provide basic information about the mechanisms of action of a variety of biologically active molecules. Addressing principles, methods, and applications, this book provides a critical selection of solid-state NMR methods for solving a wide range of practical problems that arise in both academic and industrial research of biomolecules in the solid state. NMR Spectroscopy of Biological Solids is a forward-thinking resource for students and researchers in analytical chemistry, bioengineering, material sciences, and structural genomics.