Application and Development of Multidimensional NMR Spectroscopy in Structural Studies of Oligonucleotides and Proteins PDF Download
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Author: Hong Wang
Publisher:
ISBN:
Category :
Languages : en
Pages : 402
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Book Description
Author: Hong Wang
Publisher:
ISBN:
Category :
Languages : en
Pages : 402
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Book Description
Author: Clore
Publisher: CRC Press
ISBN: 9780849377716
Category : Medical
Languages : en
Pages : 328
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Book Description
Determination of structures of larger proteins in solution by three- and four-dimensional heteronuclear magnetic resonance spectroscopy. Methodological advances in protein NMR. Determination of high-resolution NMR structures of proteins. Multidimensional NMR studies of immunosuppressant/immunophilin complexes. NMR studies of the structure and role of modules involved in protein-protein interactions. NMR structural studies of membrane proteins. Heteronuclear NMR studies of the molecular synamics of staphylococcal nuclease. Study of protein dynamics by NMR. The folding, stability and dynamics of T4 lysozyme: a perspective using nuclear magnetic resonance.
Author: Kurt Wthrich
Publisher: World Scientific
ISBN: 9789810223847
Category : Science
Languages : en
Pages : 770
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Book Description
The volume presents a survey of the research by Kurt Wthrich and his associates during the period 1965 to 1994. A selection of reprints of original papers on the use of NMR spectroscopy in structural biology is supplemented with an introduction, which outlines the foundations and the historical development of the use of NMR spectroscopy for the determination of three-dimensional structures of biological macromolecules in solution. The original papers are presented in groups highlighting protein structure determination by NMR, studies of dynamic properties and hydration of biological macromolecules, and practical applications of the NMR methodology in fields such as enzymology, transcriptional regulation, immunosuppression and protein folding.
Author: John W. Finley
Publisher: Springer Science & Business Media
ISBN: 146845868X
Category : Science
Languages : en
Pages : 512
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Book Description
Elucidating the structures of biopolymers as they exist in nature has long been a goal of biochemists and biologists. Understanding how these substances interact with themselves, other solutes, and solvents can provide useful insights into many areas of biochemistry, agriculture, food science and medicine. Knowledge of the structure of a protein or complex carbohydrate in its native form provides guidelines for the chemical or genetic modifications often desired to optimize these compounds to specific needs and applications. For example, in the pharmaceutical industry, structure-function relationships involving biopolymers are studied rou tinely as a means to design new drugs and improve their efficacies. The tools to conduct structure investigations of biopolymers at the molecular level are limited in number. Historically X-ray crystallography has been the most attractive method to conduct studies of this type. How ever, X-ray methods can only be applied to highly ordered, crystalline materials, thus obviating studies of solution dynamics that are often critical to attaining a global understanding of biopolymer behavior. In recent years, nuclear magnetic resonance (NMR) spectroscopy has evolved to become a powerful tool to probe the structures of biopolymers in solution and in the solid state. NMR provides a means to study the dynamics of polymers in solution, and to examine the effects of solute, solvent and' other factors~n polymer behavior. With the development of 2D and 3D forms of NMR spectroscopy, it is now possible to assess the solution conforma tions of small proteins, oligonucleotides and oligosaccharides.
Author: Jeffrey C. Hoch
Publisher: Springer
ISBN:
Category : Medical
Languages : en
Pages : 488
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Book Description
Without computers - no modern NMR; Parametric estimation in 1-D, 2-D, and 3-D NMR; Computational aspects of multinuclear NMR spectroscopy of proteins at NMRFAM; Principles of multidimensional NMR techniques for measurement of J coupling constants; Comparison of the NMR and X-ray structures of hirudin; The application of the linear prediction principle to NMR spectroscopy; NMR data processing and structure calculations using parallel computers; Software approaches for determination of 3-dimensional molecular structures from multi-dimensional NMR; Applicability and limitations of three-dimensional NMR spectroscopy for the study of proteins in solution; The role of selective two-dimensional NMR correlation methods in supplementing computer-supported multiplet analysis by MARCO POLO; Application of maximum entropy methods to NMR spectra of proteins; Pattern recognition in two-dimensional NMR spectra of proteins; The application and development of software tools for the processinf and analysis of heteronuclear multi-dimensional NMR data; Distance geometry in torsion angle space: new developments and applications; Structure determination by NMR: the modeling of NMR parameters as ensemble averages; Time averaged distance restraints in NMR based structural refinement; Analysis of backbone dynamics of interleukin-1 beta; A new version of DADAS (Distance Analysis in Dihedral Angle Space) and its performance; An amateur looks at error analysis in the determination of protein structure by NMR; Structural interpretation of NMR data in the presence of motion; New interactive and automatic algorithms for the assignment of NMR spectra; Outline of a computer program for the analysis of protein NMR spectra; Assignment of the NMR spectra of homologous proteins; Incorporation of internal motion in NMR refinements based on NOESY data; Refinement of three-dimensional protein and DNA structures in solution from NMR data; How to deal with spin-diffusion and internal mobility in biomolecules: a relaxation matrix approach; Interactive computer graphics in the assignment of protein 2D and 3D NMR spectra; Determination of large protein structures from NMR data: definition of the solution structure of the TRP repressor; Interpretation of NMR data in terms of protein structure: summary of a round table discussion; Fast calculation of the relaxation matrix; NMR structures of proteins using stereospecific assignments and relaxation matrix refinement in a hybrid method of distance geometry and simulated annealing; A critique of the interpretation of nuclear Overhauser effects of duplex DNA; Improvement in resolution with nonlinear methods applied to NMR signals from macromolecules; STELLA and CLAIRE: a seraglio of programs for human-aided assignment of 2D 1H NMR spectra of proteins; MolSkop: towards NMR molecular scope; Ribonuclease H: full assignment of backbone proton resonances with heteronuclear 3D NMR and solution structure; Sampling properties of simulated annealing and distance geometry.
Author: Gordon S. Rule
Publisher: Springer Science & Business Media
ISBN: 1402035004
Category : Science
Languages : en
Pages : 543
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Book Description
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: Lu-Yun Lian
Publisher: John Wiley & Sons
ISBN: 1119972825
Category : Science
Languages : en
Pages : 345
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Book Description
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.
Author: Robert Thompson Clubb
Publisher:
ISBN:
Category :
Languages : en
Pages : 458
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Book Description
Author: John Cavanagh
Publisher: Elsevier
ISBN: 008047103X
Category : Science
Languages : en
Pages : 915
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Book Description
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: B.D.N. Rao
Publisher: Springer
ISBN:
Category : Literary Collections
Languages : en
Pages : 408
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Book Description
The contemplation of truth and beauty is the proper object for which we were created, which calls forth the most intense desires of the soul, and of which it never tires -Hazlitt In his Nobel lecture Purcell commented that when he saw snow in New England after the discovery of NMR, it appeared like "heaps of protons quietly precessing in earth's magnetic field. " If he were to make the comment in the context of how NMR is being used today, he could have conjured up an image of hydrogen, carbon, and nitrogen nuclei in proteins of an earthbound 8rganism subtly orchestrating a quiet symphony of frequencies, from 150 Hz to 2 kHz, carrying clues to the three-dimensional structure of the macromolecules. The manner in which the basic discoveries of Bloch and Purcell have led to the emergence of NMR, several decades later, as a major technique of biological and medical physics (and chemistry) is a striking example of the power of basic research. It is also a fascinating saga whereby whenever it was felt that the field had reached a plateau, new directions, new technologies, and sometimes serendipity produced new developments that revolutionized the technique and enhanced its capability. As Richard Ernst points out "NMR is intellectually attractive, . . . the practical importance of NMR is enormous, and can justify much of the playful activities of an addicted spectroscopist" (Nobel lecture).
