Automatic 13 C chemical shift reference correction for unassigned protein NMR spectra
Automatic 13 C chemical shift reference correction for unassigned protein NMR spectra
Abstract
Poor chemical shift referencing, especially for 13C in protein Nuclear Magnetic Resonance (NMR) experiments, fundamentally limits and even prevents effective study of biomacromolecules via NMR, including protein structure determination and analysis of protein dynamics. To solve this problem, we constructed a Bayesian probabilistic framework that circumvents the limitations of previous reference correction methods that required protein resonance...
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11-25-2018 06:02 AM
[NMR paper] Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics.
Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics.
Related Articles Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics.
J Struct Biol. 2015 Jul 20;
Authors: Vögeli B, Olsson S, Riek R, Güntert P
Abstract
The study of the spatial sampling of biomolecules is essential to understanding the structure-dynamics-function relationship. We have established a protocol for the determination of...
nmrlearner
Journal club
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07-25-2015 01:54 PM
Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics
Complementarity and congruence between exact NOEs and traditional NMR probes for spatial decoding of protein dynamics
Publication date: Available online 20 July 2015
Source:Journal of Structural Biology</br>
Author(s): Beat Vögeli, Simon Olsson, Roland Riek, Peter Güntert</br>
The study of the spatial sampling of biomolecules is essential to understanding the structure-dynamics-function relationship. We have established a protocol for the determination of multiple-state ensembles based on exact measurements of the nuclear Overhauser effect (eNOE). The...
[NMR images] Traditional NMR uses coils to
http://michaelgr.files.wordpress.com/2007/05/nmr-protein-001.jpg?w=450
http://michaelgr.com/2007/05/24/look-at-them-proteins-a-better-nuclear-magnetic-resonance-probe-and-a-look-at-computational-protein-research/
20/12/2011 4:11:48 PM GMT
Traditional NMR uses coils to
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nmrlearner
NMR pictures
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01-12-2012 09:30 PM
SHIFTCOR: Protein Chemical Shift Re-referencing
SHIFTCOR website
SHIFTCOR is an automated shift correction program that uses statistical methods to compare and correct SHIFTX-predicted shifts relative to an input set of observed chemical shifts. SHIFTCOR uses several simple statistical approaches and pre-determined cutoff values to identify and correct potential referencing, assignment and typographical errors. SHIFTCOR identifies potential chemical shift referencing problems by comparing the difference between the average value of each set (1Hα, 13Cα, 13Cβ, 13CO, 15N and 1HN) of observed and predicted chemical shifts. The difference...
gwnmr
NMR software
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01-10-2012 06:46 PM
[NMR paper] Rapid protein fold determination using unassigned NMR data.
Rapid protein fold determination using unassigned NMR data.
Related Articles Rapid protein fold determination using unassigned NMR data.
Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15404-9
Authors: Meiler J, Baker D
Experimental structure determination by x-ray crystallography and NMR spectroscopy is slow and time-consuming compared with the rate at which new protein sequences are being identified. NMR spectroscopy has the advantage of rapidly providing the structurally relevant information in the form of unassigned chemical shifts (CSs),...
Overview of traditional and Unassigned BaMORC protein NMR referencing... - ResearchGate
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