Nuclear Magnetic Resonance Relaxation Modeling and Molecular Dynamics Simulation Studies of Protein Dynamics PDF Download
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Author: Danqing Jin
Publisher:
ISBN:
Category :
Languages : en
Pages : 122
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Book Description
Author: Danqing Jin
Publisher:
ISBN:
Category :
Languages : en
Pages : 122
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Book Description
Author: Kevin H. Mayo
Publisher:
ISBN: 9781860940767
Category : Science
Languages : en
Pages : 300
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Book Description
This book specifically addresses the use of (13)C and (15)N NMR spectroscopy to derive information on the internal motions of proteins and peptides in solution. Basic methods of NMR relaxation, along with the general theory of correlation functions and spectral densities, are first covered, followed by in-depth analyses and comparisons of various motional models and molecular dynamics simulations used to derive protein dynamics information from NMR relaxation experiments. Motional model equations are expressed in computer program-ready format. The text is ideally suited for graduate and post-graduate students as well as experienced professionals.
Author: Yuxi Pang
Publisher:
ISBN:
Category :
Languages : en
Pages : 320
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Book Description
Author: N. Rama Krishna
Publisher: Springer Science & Business Media
ISBN: 0306459531
Category : Medical
Languages : en
Pages : 565
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Book Description
Volume 17 is the second in a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series. Volume 16, with the subtitle Modern Techniques in Protein NMR , is the first in this series. These two volumes present some of the recent, significant advances in the biomolecular NMR field with emphasis on developments during the last five years. We are honored to have brought together in these volume some of the world s foremost experts who have provided broad leadership in advancing this field. Volume 16 contains - vances in two broad categories: I. Large Proteins, Complexes, and Membrane Proteins and II. Pulse Methods. Volume 17 contains major advances in: I. Com- tational Methods and II. Structure and Dynamics. The opening chapter of volume 17 starts with a consideration of some important aspects of modeling from spectroscopic and diffraction data by Wilfred van Gunsteren and his colleagues. The next two chapters deal with combined automated assignments and protein structure determination, an area of intense research in many laboratories since the traditional manual methods are often inadequate or laborious in handling large volumes of NMR data on large proteins. First, Werner Braun and his associates describe their experience with the NOAH/DIAMOD protocol developed in their laboratory.
Author: Jeffrey W. Peng
Publisher:
ISBN:
Category :
Languages : en
Pages : 562
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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: Andrew Hsu
Publisher:
ISBN:
Category :
Languages : en
Pages :
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Book Description
We derive the inverse Gaussian probability distribution function from general properties of spectral density functions at low and high frequencies for macromolecules in solution, using the principle of maximum entropy. The resulting model-free spectral density functions are finite at a frequency of zero and can be used to describe distributions of either overall or internal correlation times using the model-free ansatz. The approach is validated using 15N backbone relaxation data for the intrinsically disordered, DNA-binding region of the bZip transcription factor domain of the Saccharomyces cerevisiae protein GCN4, in the absence of cognate DNA.
Author: Rainer Kimmich
Publisher: Royal Society of Chemistry
ISBN: 1788015509
Category : Science
Languages : en
Pages : 590
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Book Description
Field-cycling NMR relaxometry is evolving into a methodology of widespread interest with recent technological developments resulting in powerful and versatile commercial instruments. Polymers, liquid crystals, biomaterials, porous media, tissue, cement and many other materials of practical importance can be studied using this technique. This book summarises the expertise of leading scientists in the area and the editor is well placed, after four decades of working in this field, to ensure a broad ranging and high quality title. Starting with an overview of the basic principles of the technique and the scope of its use, the content then develops to look at theory, instrumentation, practical limitations and applications in different systems. Newcomers to the field will find this book invaluable for successful use of the technique. Researchers already in academic and industrial settings, interested in molecular dynamics and magnetic resonance, will discover an important addition to the literature.
Author: Aron W. Fenton
Publisher: Humana Press
ISBN: 9781617793332
Category : Science
Languages : en
Pages : 0
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Book Description
Despite considerable variability within the scientific community, allosteric regulation can best be defined functionally as how a macromolecule binds one ligand differently when a second ligand is or is not pre-bound to the macromolecule, which constitutes a vital aspect of protein structure/function. In Allostery: Methods and Protocols, expert researchers in the field provide key techniques to investigate this biological phenomenon. Focusing on heterotropic systems with some coverage of homotropic systems, this volume covers the monitoring of allosteric function, allosteric conformational changes, and allosteric changes in protein dynamics/sub-population distribution, as well as topics such as macromolecular and ligand engineering of allosteric functions and computational aids in the study of allostery. Written in the highly successful Methods in Molecular BiologyTM series format, the chapters include the kind of detailed description and implementation advice that is crucial for getting optimal results in the laboratory. Thorough and intuitive, Allostery: Methods and Protocols aids scientists in continuing to study ligand-induced, through-protein effects on protein function (ligand binding/catalysis), a phenomenon that is well recognized through the history of the life sciences and very poorly understood at the molecular level.
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.
