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[Encyclopedia.of.Life.Sciences].[Encyclopedia.of.Life.Sciences].[Encyclopedia.of.Life.Sciences].Nuclear.ic.Resonance.(NMR).Spectroscopy.for.Monitoring.pdf

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[Encyclopedia.of.Life.Sciences].[Encyclopedia.of.Life.Sciences].[Encyclopedia.of.Life.Sciences].Nuclear.ic.Resonance.(NMR).Spectroscopy.for.Monitoring.pdf

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[Encyclopedia.of.Life.Sciences].[Encyclopedia.of.Life.Sciences].[Encyclopedia.of.Life.Sciences].Nuclear.ic.Resonance.(NMR).Spectroscopy.for.Monitoring.pdf

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文档介绍:NMR Spectroscopy for Secondary article
Monitoring Molecular Article Contents
. Introduction
Dynamics in Solution . Isotopic Enrichment for Relaxation Studies
. Theory of Relaxation
Andrew L Lee, University of Pennsylvania, Philadelphia, Pennsylvania, USA . NMR Relaxation Measurements
. Interpretation of Relaxation Parameters
A Joshua Wand, University of Pennsylvania, Philadelphia, Pennsylvania, USA
. Backbone Dynamics in Proteins
. Side-chain Dynamics in Proteins
Biological macromolecules exhibit a wide range of dynamic motions. Analysis of relaxation
. Expanding the Range of Dynamic Information
rates of NMR signals allows these motions to be characterized throughout a
. Dynamics and Entropy
macromolecule at an atomic level of detail.
Introduction
dynamics of the backbone of a protein, analysis of amide
15N relaxation rates is the most convenient approach and
Nuclear ic resonance (NMR) spectroscopy is a 15
powerful tool for characterizing structure and dynamics in requires uniform N enrichment of the protein. For access
to protein side-chain dynamics, various approaches to 13C
biological macromolecules. Although other techniques, 2
such as X-ray crystallography, can also determine high- and H relaxation rely on uniform or specific labelling
patterns, usually attainable in a bacterial expression
resolution structures, NMR is uniquely suited to t