Nuclear Magnetic Resonance Studies of Side-chain Motions in Calbindin D9k PDF Download
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Author: Eric Michael Johnson
Publisher:
ISBN:
Category :
Languages : en
Pages : 147
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Book Description
An accurate understanding of the role of conformational dynamics in proteins requires data at multiple timescales and sites within the protein of interest. Considerable progress has been achieved in characterizing the picosecond-to-nanosecond (ps-ns) dynamics of the protein backbone via NMR relaxation measurements of the 15N nucleus. More recent developments in the measurement of 2H quadrupolar relaxation rates are enabling an extensive characterization of the dynamics in methyl-containing side-chains as well. The aim of the present study is to characterize the effects of Ca2+ binding on the side-chain dynamics of the protein calbindin D9k. Calbindin is a small (~8.7 kD), single domain protein of the EF-hand family. It contains two Ca2+ binding sites that exhibit high positive cooperativity. Longitudinal, transverse, quadrupolar order, transverse antiphase and double quantum relaxation rates are reported for both the apo (Ca2+-free) and Ca2+-loaded states of the protein at two magnetic field strengths. The relatively large size of the data set allows for a detailed analysis of the underlying conformational dynamics by spectral density mapping and model-free fitting procedures. The results indicate that a methyl group's distance from the Ca2+ binding sites is a significant determinant of its conformational dynamics. Several methyl groups segregate into two limiting classes, one proximal and the other distal to the binding sites. Methyl groups in these two classes respond differently to Ca2+ binding, both in terms of the timescale and amplitude of their fluctuations. Ca2+ binding elicits a partial immobilization among methyl groups in the proximal class, which is consistent with previous studies of calbindin's backbone dynamics. The distal class, however, exhibits a trend that could not be inferred from the backbone data in that its mobility actually increases with Ca2+ binding. We have introduced the term polar dynamics to describe this type of organization across the molecule. The trend may represent an important mechanism by which calbindin achieves high affinity binding while minimizing the corresponding conformational entropy loss.
Author: Eric Michael Johnson
Publisher:
ISBN:
Category :
Languages : en
Pages : 147
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Book Description
An accurate understanding of the role of conformational dynamics in proteins requires data at multiple timescales and sites within the protein of interest. Considerable progress has been achieved in characterizing the picosecond-to-nanosecond (ps-ns) dynamics of the protein backbone via NMR relaxation measurements of the 15N nucleus. More recent developments in the measurement of 2H quadrupolar relaxation rates are enabling an extensive characterization of the dynamics in methyl-containing side-chains as well. The aim of the present study is to characterize the effects of Ca2+ binding on the side-chain dynamics of the protein calbindin D9k. Calbindin is a small (~8.7 kD), single domain protein of the EF-hand family. It contains two Ca2+ binding sites that exhibit high positive cooperativity. Longitudinal, transverse, quadrupolar order, transverse antiphase and double quantum relaxation rates are reported for both the apo (Ca2+-free) and Ca2+-loaded states of the protein at two magnetic field strengths. The relatively large size of the data set allows for a detailed analysis of the underlying conformational dynamics by spectral density mapping and model-free fitting procedures. The results indicate that a methyl group's distance from the Ca2+ binding sites is a significant determinant of its conformational dynamics. Several methyl groups segregate into two limiting classes, one proximal and the other distal to the binding sites. Methyl groups in these two classes respond differently to Ca2+ binding, both in terms of the timescale and amplitude of their fluctuations. Ca2+ binding elicits a partial immobilization among methyl groups in the proximal class, which is consistent with previous studies of calbindin's backbone dynamics. The distal class, however, exhibits a trend that could not be inferred from the backbone data in that its mobility actually increases with Ca2+ binding. We have introduced the term polar dynamics to describe this type of organization across the molecule. The trend may represent an important mechanism by which calbindin achieves high affinity binding while minimizing the corresponding conformational entropy loss.
Author: Johan Evenäs
Publisher:
ISBN:
Category : Calmodulin
Languages : en
Pages : 122
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Book Description
Author: Tak Yan Tse
Publisher:
ISBN:
Category : Deuteron magnetic resonance spectroscopy
Languages : en
Pages : 340
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Book Description
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages :
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Book Description
Author: The Nuclear Magnetic Resonance Society of Japan
Publisher: Springer
ISBN: 9811059667
Category : Science
Languages : en
Pages : 634
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Book Description
This book describes the advanced developments in methodology and applications of NMR spectroscopy to life science and materials science. Experts who are leaders in the development of new methods and applications of life and material sciences have contributed an exciting range of topics that cover recent advances in structural determination of biological and material molecules, dynamic aspects of biological and material molecules, and development of novel NMR techniques, including resolution and sensitivity enhancement. First, this book particularly emphasizes the experimental details for new researchers to use NMR spectroscopy and pick up the potentials of NMR spectroscopy. Second, the book is designed for those who are involved in either developing the technique or expanding the NMR application fields by applying them to specific samples. Third, the Nuclear Magnetic Resonance Society of Japan has organized this book not only for NMR members of Japan but also for readers worldwide who are interested in using NMR spectroscopy extensively.
Author: G. A. Webb
Publisher: Royal Society of Chemistry
ISBN: 0854043624
Category : Medical
Languages : en
Pages : 419
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Book Description
Annotation As a spectroscopic method, Nuclear Magnetic Resonance (NMR) has seen spectacular growth over the past two decades, both as a technique and in its applications. Today the applications of NMR span a wide range of scientific disciplines, from physics to biology to medicine. Each volume of Nuclear Magnetic Resonance comprises a combination of annual and biennial reports which together provide comprehensive coverage of the literature on this topic. For those wanting to become rapidly acquainted with specific areas of NMR, this title provides unrivalled scope of coverage. Seasoned practitioners of NMR will find this an invaluable source of current methods and applications. Each volume of Nuclear Magnetic Resonance comprises a combination of annual and biennial reports which together provide comprehensive of the literature on this topic. This Specialist Periodical Report reflects the growing volume of published work involving NMR techniques and applications, in particular NMR of natural macromolecules which is covered in two reports: "NMR of Proteins and Acids" and "NMR of Carbohydrates, Lipids and Membranes". For those wanting to become rapidly acquainted with specific areas of NMR, this title provides unrivalled scope of coverage. Seasoned practitioners of NMR will find this an in valuable source of current methods and applications. Specialist Periodical Reports provide systematic and detailed review coverage in major areas of chemical research. Compiled by teams of leading authorities in the relevant subject areas, the series creates a unique service for the active research chemist, with regular, in-depth accounts of progress in particular fields of chemistry. Subject coverage within different volumes of a given title is similar and publication is on an annual or biennial basis.
Author: Ronald Reid
Publisher: CRC Press
ISBN: 9781420001334
Category : Medical
Languages : en
Pages : 918
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Book Description
Furthering efforts to simulate the potency and specificity exhibited by peptides and proteins in healthy cells, this remarkable reference supplies pharmaceutical scientists with a wealth of techniques for tapping the enormous therapeutic potential of these molecules-providing a solid basis of knowledge for new drug design. Provides a broad, comprehensive overview of peptides and proteins as mediators of cell movement, proliferation, differentiation, and communication. Written by more than 50 leading international authorities, Peptides and Protein Drug Analysis discusses strategies for dealing with the complexity of peptides and proteins in conformational flexibility and amino acid sequence variability analyzes drug formulations facilitated by solid-phase peptide synthesis and recombinant DNA technology examines chemical purity analysis by high-pressure chromatographic, capillary electrophoretic, gel electrophoretic, and isoelectric focusing methods highlights drug design elements derived from protein folding, bioinformatics, and computational chemistry demonstrates uses of unnatural mutagenesis and combinatorial chemistry explores mass spectrometry, protein sequence, and carbohydrate analysis illustrates bioassays and other new functional analysis methods surveys spectroscopic techniques such as ultraviolet, fluorescence, Fourier transform infrared, and nuclear magnetic resonance (NMR) addresses ways of distinguishing between levels of therapeutic and endogenous agents in cells reviews structural analysis tools such as ultracentrifugation and light, X-ray, and neutron scattering and more! Featuring over 3400 bibliographic citations and more than 500 tables, equations, and illustrations, Peptide and Protein Drug Analysis is a must-read resource for pharmacists; pharmacologists; analytical, organic, and pharmaceutical chemists; cell and molecular biologists; biochemists; and upper-level undergraduate and graduate students in these disciplines.
Author: O. Jardetsky
Publisher: Springer Science & Business Media
ISBN: 1468457454
Category : Science
Languages : en
Pages : 383
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Book Description
Proceedings of the Tenth Course of the International School of Pure and Applied Biostructure (Erice, Italy, June 1989). Knowledge of protein structure and of design and manufacture methods has made it possible to produce proteins of any desired sequence, but progress is limited by inability to predi
Author:
Publisher:
ISBN:
Category : Dissertations, Academic
Languages : en
Pages : 860
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Book Description
Author: Yutaka Ito
Publisher: Royal Society of Chemistry
ISBN: 1839160934
Category : Science
Languages : en
Pages : 322
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Book Description
In-cell NMR spectroscopy is a relatively new field. Despite its short history, recent in-cell NMR-related publications in major journals indicate that this method is receiving significant general attention. This book provides the first informative work specifically focused on in-cell NMR. It details the historical background of in-cell NMR, host cells for in-cell NMR studies, methods for in-cell biological techniques and NMR spectroscopy, applications, and future perspectives. Researchers in biochemistry, biophysics, molecular biology, cell biology, structural biology as well as NMR analysts interested in biological applications will all find this book valuable reading.
