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eBook Protein Dynamics NMR Relaxation epub

by Kevin H. Mayo,Vladimir A. Daragan

eBook Protein Dynamics NMR Relaxation epub
  • ISBN: 1860940765
  • Author: Kevin H. Mayo,Vladimir A. Daragan
  • Genre: Science
  • Subcategory: Biological Sciences
  • Language: English
  • Publisher: Imperial College Pr; 1st edition (December 31, 2014)
  • Pages: 300 pages
  • ePUB size: 1411 kb
  • FB2 size 1845 kb
  • Formats doc docx lrf lit


Vladimir A. Daragan, Kevin H. Mayo. A novel approach is described to analyze NMR relaxation data on proteins.

Vladimir A. Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiplet relaxation study. Specific binding of ethanol to cholesterol in organic solvents.

A novel approach is described to analyze NMR relaxation data on proteins. A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13C NMR relaxation data is presented.

Lysine side-chain dynamics derived from 13C-multiplet NMR relaxation studies . Dmitry Mikhailov, Vladimir A. Mayo Pages 397-410.

Lysine side-chain dynamics derived from 13C-multiplet NMR relaxation studies on di- and tripeptides. Short Communications. Assignment of the backbone carbonyl resonances in 15N-labelled proteins with 13C at natural abundance by a 2D triple-resonance correlation technique. Søren M. Kristensen, Morten Dahl Sørensen, Jens J. Led Pages 411-414. Probing internal water molecules in proteins using two-dimensional 19F-1H NMR.

Djaudat Idiyatullin Vladimir A Daragan Kevin H Mayo. J Magn Reson 2003 Mar;161(1):118-25. S(2)(omega) is defined as the sum of a specified set of weighting coefficients from the Lorentzian expansion of the spectral density function. 15N NMR relaxation data (500, 600, and 800 MHz) on protein GB1 exemplify the method. daragan, luis serrano, kevin h. mayo These data support the Daragan–Mayo model of correlated bond rotations (Daragan V. .

Djaudat idiyatullin, alexei krushelnitsky, irina nesmelova, francesco blanco, vladimir a. Journal: Protein Science, Volume 9, Issue 11, November 2000. To investigate backbone and side-chain internal motions within the helix and hydrophobic staple, residues F2, A5, L7, A8, and A10 were selectively 13C- and 15N-enriched and NMR relaxation experiments were performed in water and in ol (TFE) solution at four Larmor frequencies (6., 125, 150, and 200 MHz for 13C)

Vladimir A. Published: 1 February 1996. by Elsevier BV. in Journal of Magnetic Resonance, Series B. Journal of Magnetic Resonance, Series B, Volume 110, pp 164-175; doi:10. For questions or feedback, please reach us at support at scilit.

In magnetic resonance imaging (MRI) and nuclear magnetic resonance spectroscopy (NMR spectroscopy), the term relaxation describes how signals change with time. In general signals deteriorate with time, becoming weaker and broader. The deterioration reflects the fact that the NMR signal, which results from nuclear magnetization, arises from the over-population of an excited state. Relaxation is the conversion of this non-equilibrium population to a normal population.

Protein Dynamics: A Study of the Model-free Analysis of NMR Relaxation Data. by Edward d''Auvergne (Author).

Here, we focus on 15N R1ρ experiments for protein NH groups. We present protocols for both on- and off-resonance 15N R1ρ measurements needed for relaxation dispersion studies, and describe the data analysis for extracting kinetic and thermodynamic parameters characterizing the motional processes.

The book assumes only a basic knowledge of complex numbers and matrices, and provides the reader with .

The book assumes only a basic knowledge of complex numbers and matrices, and provides the reader with numerous worked examples and exercises to encourage understanding. With the explicit aim of carefully developing the subject from the beginning, the text starts with coverage of quarks and nucleons and progresses through to a detailed explanation of several important NMR experiments, including NMR imaging, COSY, NOESY and TROSY.

This volume addresses the use of 13C and 15N 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 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 intended for graduate and post-graduate students as well as professionals.
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