Related ArticlesInformation content of long-range NMR data for the characterization of conformational heterogeneity.
J Biomol NMR. 2015 Jun 5;
Authors: Andra?oj? W, Berlin K, Fushman D, Luchinat C, Parigi G, Ravera E, Sgheri L
Abstract
Long-range NMR data, namely residual dipolar couplings (RDCs) from external alignment and paramagnetic data, are becoming increasingly popular for the characterization of conformational heterogeneity of multidomain biomacromolecules and protein complexes. The question addressed here is how much information is contained in these averaged data. We have analyzed and compared the information content of conformationally averaged RDCs caused by steric alignment and of both RDCs and pseudocontact shifts caused by paramagnetic alignment, and found that, despite the substantial differences, they contain a similar amount of information. Furthermore, using several synthetic tests we find that both sets of data are equally good towards recovering the major state(s) in conformational distributions.
PMID: 26044033 [PubMed - as supplied by publisher]
Information content of long-range NMR data for the characterization of conformational heterogeneity
Information content of long-range NMR data for the characterization of conformational heterogeneity
Abstract
Long-range NMR data, namely residual dipolar couplings (RDCs) from external alignment and paramagnetic data, are becoming increasingly popular for the characterization of conformational heterogeneity of multidomain biomacromolecules and protein complexes. The question addressed here is how much information is contained in these averaged data. We have analyzed and compared the information content of conformationally averaged RDCs caused by...
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06-05-2015 01:10 AM
[U. of Ottawa NMR Facility Blog] The Information Content of an FID
The Information Content of an FID
The free induction decay (FID) is a function representing the decay of transverse magnetization as a function of time after the application of a pulse (or pulse sequence). The NMR spectrum is obtained by Fourier transforming the FID. All of the information in the NMR spectrum (line width, intensity, phase, line shape ....) is contained in the FID. Knowledge of what part of the FID represents a particular property of an NMR spectrum allows a user to process the raw time domain data in a way that maximizes the quality and information content of the...
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04-17-2015 08:49 PM
[NMR paper] Sparse labeling of proteins: Structural characterization from long range constraints
Sparse labeling of proteins: Structural characterization from long range constraints
Publication date: April 2014
Source:Journal of Magnetic Resonance, Volume 241</br>
Author(s): James H. Prestegard , David A. Agard , Kelley W. Moremen , Laura A. Lavery , Laura C. Morris , Kari Pederson</br>
Structural characterization of biologically important proteins faces many challenges associated with degradation of resolution as molecular size increases and loss of resolution improving tools such as perdeuteration when non-bacterial hosts must be used for expression. In...
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03-22-2014 01:28 AM
[Question from NMRWiki Q&A forum] Long-range 1H-{15N} coupling (HMBC)
Long-range 1H-{15N} coupling (HMBC)
Hello All
I have two examples of what appears to be 6J coupling between 1H and 15N using gradient HMBC experiments with 15N at natural abundance. For such an experiment, 2J and 3J correlations are typical, sometimes 4J (W-type) but I've never seen 6J before.
Has anyone else ever seen correlations over this distance? Any other comments?
Craig.
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10-29-2012 07:03 PM
[U. of Ottawa NMR Facility Blog] Measurement of Long Range C H Coupling Constants
Measurement of Long Range C H Coupling Constants
The stereochemistry of compounds is assigned very often with proton - proton NOE's by applying the 2D NOESY technique or the 1D selective gradient NOESY technique. These methods fail, however when the distance between protons is too large to measure an NOE. When faced with this situation, it may be possible to measure long range proton - carbon coupling constants which are able to provide the necessary information. Three-bond carbon - proton couplings follow a Karplus relationship where the magnitude of the coupling constant is related to...
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08-17-2012 10:44 PM
Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data
Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data
Yi Xue, Joshua M. Ward, Tairan Yuwen, Ivan S. Podkorytov and Nikolai R. Skrynnikov
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206442c/aop/images/medium/ja-2011-06442c_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206442c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/NvRRKHU2H3k
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01-28-2012 05:27 AM
[NMR paper] Conformational heterogeneity of transmembrane residues after the Schiff base reproton
Conformational heterogeneity of transmembrane residues after the Schiff base reprotonation of bacteriorhodopsin: 15N CPMAS NMR of D85N/T170C membranes.
Related Articles Conformational heterogeneity of transmembrane residues after the Schiff base reprotonation of bacteriorhodopsin: 15N CPMAS NMR of D85N/T170C membranes.
FEBS J. 2005 May;272(9):2152-64
Authors: Mason AJ, Turner GJ, Glaubitz C
bR, N-like and O-like intermediate states of methionine-labelled wild type and D85N/T170C bacteriorhodopsin were accumulated in native membranes by...
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11-25-2010 08:21 PM
[NMR paper] Exploring the dynamic information content of a protein NMR structure: comparison of a
Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
Proteins. 1999 Jul 1;36(1):87-110
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Information content of long-range NMR data for the characterization of conformational heterogeneity.
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