Dynamics of Biological Macromolecules as Probed by NMR PDF Download
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Author: Heike Blad
Publisher:
ISBN:
Category :
Languages : en
Pages : 190
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Book Description
Author: Heike Blad
Publisher:
ISBN:
Category :
Languages : en
Pages : 190
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Book Description
Author: Anirban Bhunia
Publisher: Royal Society of Chemistry
ISBN: 1839165715
Category : Science
Languages : en
Pages : 733
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Book Description
NMR spectroscopy has found a wide range of applications in life sciences over recent decades. Providing a comprehensive amalgamation of the scattered knowledge of how to apply high-resolution NMR techniques to biomolecular systems, this book will break down the conventional stereotypes in the use of NMR for structural studies. The major focus is on novel approaches in NMR which deal with the functional interface of either protein-protein interactions or protein-lipid interactions. Bridging the gaps between structural and functional studies, the Editors believe a thorough compilation of these studies will open an entirely new dimension of understanding of crucial functional motifs. This in turn will be helpful for future applications into drug design or better understanding of systems. The book will appeal to NMR practitioners in industry and academia who are looking for a comprehensive understanding of the possibilities of applying high-resolution NMR spectroscopic techniques in probing biomolecular interactions.
Author: Chariklia I. Stassinopoulou
Publisher: Springer Science & Business Media
ISBN: 3642791581
Category : Science
Languages : en
Pages : 367
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Book Description
Provided here are the latest techniques of NMR as applied to the study of proteins, carbohydrates and nucleic acids. The first chapters are devoted to an introduction to NMR and parameters related to molecular structure and molecular interactions. NMR experiments from basic 1D to 2D, 3D and 4D, used in combination with isotopically labelled molecules, are described and a general strategy is presented for biomacromolecular structure determination. Subsequent chapters deal with more advanced principles and techniques and their applications to structural and dynamic processes involving biomacromolecules in solution. Advanced results on peptide, protein, oligosaccharide and nucleic acid structure and recognition are presented.
Author: John L. Markley
Publisher: Oxford University Press
ISBN: 0195357426
Category : Science
Languages : en
Pages : 375
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Book Description
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: Andrew J. Dingley
Publisher: IOS Press
ISBN: 1607506947
Category : Medical
Languages : en
Pages : 488
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Book Description
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--
Author:
Publisher: Elsevier
ISBN: 0080496881
Category : Science
Languages : en
Pages : 513
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Book Description
This volume and its companion, Volume 339, supplement Volumes 176, 177, 239, and 261. Chapters are written with a "hands-on" perspective. That is, practical applications with critical evaluations of methodologies and experimental considerations needed to design, execute, and interpret NMR experiments pertinent to biological molecules.
Author: Ye Tian
Publisher:
ISBN: 9781124263557
Category : DNA-protein interactions
Languages : en
Pages : 147
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Book Description
Another practice of NMR in my work is using 31 P Dynamic NMR to characterize the backbone conformation and dynamics in DNA Dickerson Dodecamer. The results confirm solid-state 2 H-NMR experiments showing that the C3pG4 and C9pG10 steps experience unique dynamics. And cytosine methylation has significant impact on the local dynamics. The results also show that 31 P Dynamic NMR is an efficient way to extract DNA backbone dynamic information, and provide detail knowledge to study DNA-protein interactions.
Author: Guang Zhu
Publisher: Springer Science & Business Media
ISBN: 3642289169
Category : Science
Languages : en
Pages : 255
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Book Description
Application of NMR and Molecular Docking in Structure-Based Drug Discovery, by Jaime L. Stark and Robert Powers NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions, by Olga Vinogradova and Jun Qin The Use of Residual Dipolar Coupling in Studying Proteins by NMR, by Kang Chen und Nico Tjandra NMR Studies of Metalloproteins, by Hongyan Li and Hongzhe Sun Recent Developments in 15N NMR Relaxation Studies that Probe Protein Backbone Dynamics, by Rieko Ishima Contemporary Methods in Structure Determination of Membrane Proteins by Solution NMR, by Tabussom Qureshi and Natalie K. Goto Protein Structure Determination by Solid-State NMR, by Xin Zhao Dynamic Nuclear Polarization: New Methodology and Applications, by Kong Hung Sze, Qinglin Wu, Ho Sum Tse and Guang Zhu
Author:
Publisher: Academic Press
ISBN: 0080549470
Category : Science
Languages : en
Pages : 670
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Book Description
The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences. Nuclear Magnetic Resonance of Biological Macromolecules, Part C is written with a "hands-on" perspective. That is, practical applications with critical evaluations of methodologies and experimental considerations needed to design, execute, and interpret NMR experiments pertinent to biological molecules.* One of the most highly respected publications in the field of biochemistry since 1955 * Frequently consulted, and praised by researchers and reviewers alike * Truly an essential publication for anyone in any field of the life sciences
Author: Oleg Jardetzky
Publisher: Springer Science & Business Media
ISBN: 1461558395
Category : Science
Languages : en
Pages : 308
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Book Description
From within complex structures of organisms and cells down to the molecular level, biological processes all involve movement. Muscular fibers slide on each other to activate the muscle, as polymerases do along nucleic acids for replicating and transcribing the genetic material. Cells move and organize themselves into organs by recognizing each other through macromolecular surface-specific interactions. These recognition processes involve the mu tual adaptation of structures that rely on their flexibility. All sorts of conformational changes occur in proteins involved in through-membrane signal transmission, showing another aspect of the flexibility of these macromolecules. The movement and flexibility are inscribed in the polymeric nature of essential biological macromolecules such as proteins and nucleic acids. For instance, the well-defined structures formed by the long protein chain are held together by weak noncovalent interac tions that design a complex potential well in which the protein floats, permanently fluctuating between several micro- or macroconformations in a wide range of frequencies and ampli tudes. The inherent mobility of biomolecular edifices may be crucial to the adaptation of their structures to particular functions. Progress in methods for investigating macromolecular structures and dynamics make this hypothesis not only attractive but more and more testable.
