Spectroscopic Methods for Determining Protein Structure in Solution
Author | : Henry A. Havel |
Publisher | : VCH Publishers |
Total Pages | : 272 |
Release | : 1996 |
Genre | : Science |
ISBN | : |
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Author | : Henry A. Havel |
Publisher | : VCH Publishers |
Total Pages | : 272 |
Release | : 1996 |
Genre | : Science |
ISBN | : |
Author | : Vladimir N. Uversky |
Publisher | : Nova Publishers |
Total Pages | : 326 |
Release | : 2007 |
Genre | : Science |
ISBN | : 9781600217036 |
Protein research is a frontier field in science. Proteins are widely distributed in plants and animals and are the principal constituents of the protoplasm of all cells, and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved throughout the body, and in photosynthesis. This book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.
Author | : Bruce Alberts |
Publisher | : |
Total Pages | : 0 |
Release | : 2002 |
Genre | : Cytology |
ISBN | : 9780815332183 |
Author | : John Cavanagh |
Publisher | : Elsevier |
Total Pages | : 915 |
Release | : 2010-07-21 |
Genre | : Science |
ISBN | : 008047103X |
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 | : Clarence H. Suelter |
Publisher | : Wiley-Interscience |
Total Pages | : 310 |
Release | : 1991-01-16 |
Genre | : Science |
ISBN | : 9780471513261 |
Presents methods for determining the secondary and tertiary structure of proteins. The issues covered here involve theoretical/empirical approaches for predicting protein structure; a review using protein ligand interactions to study surface properties of proteins; use of fluorescence techniques to study structure and dynamics of proteins; and limited proteolysis with monoclonal antibodies to understand how specific structural features confer biological function.
Author | : Vladimir N. Uversky |
Publisher | : Nova Publishers |
Total Pages | : 382 |
Release | : 2007 |
Genre | : Circular dichroism |
ISBN | : 9781600214042 |
Author | : Vladimir N. Uversky |
Publisher | : Nova Publishers |
Total Pages | : 414 |
Release | : 2007 |
Genre | : Science |
ISBN | : 9781600217043 |
Protein research is a frontier field in science. Proteins are widely distributed in plants and animals and are the principal constituents of the protoplasm of all cells, and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved throughout the body, and in photosynthesis. This book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.
Author | : Robert A. Copeland |
Publisher | : Springer Science & Business Media |
Total Pages | : 238 |
Release | : 2013-11-11 |
Genre | : Science |
ISBN | : 1475715056 |
As protein science continues to become an increasingly important aspect of academic and commercial sciences and technology, the need has arisen for a ready source of laboratory protocols for the analysis and evaluation of these biological polymers. Methods for Protein Analysis presents the methods most relevant to the generalist bench scientist working with proteins. A concise yet thorough summary, it covers laboratory methods that can be reasonably performed in a standard protein laboratory, without specialized equipment or expertise. Taking a how to approach, this book examines the techniques used to answer common protein analytical questions and describes methods useful in daily laboratory work. Methods for Protein Analysis is the ideal reference for protein laboratories in academic, government and industrial settings. It is an essential benchtop manual for first-year graduate students beginning their laboratory experience as well as for chemists, biochemists, and molecular biologists in the pharmaceutical, biotechnological, food and specialty chemical industries, and for analysts concerned with the purity and structural integrity of protein. Featuring illustrations and a convenient spiral binding, this guide offers a glossary of common abbreviations and a list of suppliers for protein science.
Author | : Jennifer J. McManus |
Publisher | : Humana |
Total Pages | : 266 |
Release | : 2020-08-08 |
Genre | : Science |
ISBN | : 9781493996803 |
This volume explores experimental and computational approaches to measuring the most widely studied protein assemblies, including condensed liquid phases, aggregates, and crystals. The chapters in this book are organized into three parts: Part One looks at the techniques used to measure protein-protein interactions and equilibrium protein phases in dilute and concentrated protein solutions; Part Two describes methods to measure kinetics of aggregation and to characterize the assembled state; and Part Three details several different computational approaches that are currently used to help researchers understand protein self-assembly. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Thorough and cutting-edge, Protein Self-Assembly: Methods and Protocols is a valuable resource for researchers who are interested in learning more about this developing field.
Author | : Isao Suetake |
Publisher | : John Wiley & Sons |
Total Pages | : 245 |
Release | : 2023-03-27 |
Genre | : Science |
ISBN | : 1119886325 |
ANALYTICAL TECHNIQUES FOR THE ELUCIDATION OF PROTEIN FUNCTION An essential aid for scientists seeking alternative techniques for investigating proteins Proteins are the building blocks of living organisms, and they play an enormous range of fundamental roles in sustaining and shaping life. The critical determinant of a protein’s function is its structure, and the analysis of protein structures has therefore become a significant component of biological research. In recent years, longstanding analytical techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy have been supplemented by a number of new methods which promise to revolutionize the study of proteins and their functions. Analytical Techniques for the Elucidation of Protein Function serves as an introduction to these techniques, which are especially crucial for analyzing intrinsically disordered regions and post-translational modifications. These have revolutionized the study of proteins in recent years, and conventional methods for analyzing protein structures are no longer sufficient to work through their ramifications. This book therefore brings greater awareness of techniques which promise to produce the very cutting edge of protein research. Analytical Techniques for the Elucidation of Protein Function readers will find: A discussion of techniques including electron paramagnetic resonance (ESR) spectroscopy, neutron scattering, Raman imaging, and more Both theoretical background and practical applications for each technique Contributions from leading international researchers into protein structure and function This practically focused text is a valuable reference for protein and peptide analysis and synthesis researchers, as well as for graduate and advanced undergraduate students in the life sciences.