FRET Pursues Affordable, Robust, User-Friendly Instruments Photonics.com
... FRET-based solution structures for large and flexible proteins and their complexes, something that is quite challenging to do using standard structural biology techniques such as x-ray crystallography and NMR [nuclear magnetic resonance...
Press Release: NIH Funds Development of Integrated THz System, Making DNP-NMR Spectroscopy More Affordable
From The DNP-NMR Blog:
Press Release: NIH Funds Development of Integrated THz System, Making DNP-NMR Spectroscopy More Affordable
Press Release
NIH Funds Development of Integrated THz System, Making DNP-NMR Spectroscopy More Affordable
Bridge12’s SBIR Fast-Track Grant Will Eliminate Need for Second Superconducting Magnet, Greatly Reducing Cost for Dynamic Nuclear Polarization
nmrlearner
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11-21-2013 01:14 AM
[NMR paper] GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data.
From Mendeley Biomolecular NMR group:
GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data.
Journal of biomolecular NMR (2011). Ian R Kleckner, Mark P Foster et al.
Molecular dynamics are essential for life, and nuclear magnetic resonance (NMR) spectroscopy has been used extensively to characterize these phenomena since the 1950s. For the past 15*years, the Carr-Purcell Meiboom-Gill relaxation dispersion (CPMG RD) NMR experiment has afforded advanced NMR labs access to kinetic, thermodynamic, and structural details of protein and RNA dynamics in the...
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11-22-2012 11:49 AM
[NMR paper] GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data.
From Mendeley Biomolecular NMR group:
GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data.
Journal of biomolecular NMR (2011). Ian R Kleckner, Mark P Foster et al.
Molecular dynamics are essential for life, and nuclear magnetic resonance (NMR) spectroscopy has been used extensively to characterize these phenomena since the 1950s. For the past 15*years, the Carr-Purcell Meiboom-Gill relaxation dispersion (CPMG RD) NMR experiment has afforded advanced NMR labs access to kinetic, thermodynamic, and structural details of protein and RNA dynamics in the...
nmrlearner
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10-12-2012 09:58 AM
[NMR paper] GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data.
From Mendeley Biomolecular NMR group:
GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data.
Journal of biomolecular NMR (2011). Ian R Kleckner, Mark P Foster et al.
Molecular dynamics are essential for life, and nuclear magnetic resonance (NMR) spectroscopy has been used extensively to characterize these phenomena since the 1950s. For the past 15*years, the Carr-Purcell Meiboom-Gill relaxation dispersion (CPMG RD) NMR experiment has afforded advanced NMR labs access to kinetic, thermodynamic, and structural details of protein and RNA dynamics in the...
nmrlearner
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08-24-2012 08:01 PM
[KPWU blog] GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data
GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data
There is an article published at Journal of Biomolecular NMR recently which describes a package of MATLAB scripts to analyze CPMG relaxation dispersion NMR data. I haven’t done CPMG RD experiments on my target proteins, however, I know the analysis of CPMG RD data is not trivial. This program, GUARDD, seems to be a very http://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=629&subd=kpwu&ref=&feed=1
Go to KPWU blog to read complete post.
nmrlearner
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12-21-2011 04:12 AM
GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data
GUARDD: user-friendly MATLAB software for rigorous analysis of CPMG RD NMR data
Abstract Molecular dynamics are essential for life, and nuclear magnetic resonance (NMR) spectroscopy has been used extensively to characterize these phenomena since the 1950s. For the past 15 years, the Carr-Purcell Meiboom-Gill relaxation dispersion (CPMG RD) NMR experiment has afforded advanced NMR labs access to kinetic, thermodynamic, and structural details of protein and RNA dynamics in the crucial μs-ms time window. However, analysis of RD data is challenging because datasets are often large and...
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12-13-2011 02:46 AM
Robust structure-based resonance assignment for functional protein studies by NMR
Abstract High-throughput functional protein NMR studies, like protein interactions or dynamics, require an automated approach for the assignment of the protein backbone. With the availability of a growing number of protein 3D structures, a new class of automated approaches, called structure-based assignment, has been developed quite recently. Structure-based approaches use primarily NMR input data that are not based on J-coupling and for which connections between residues are not limited by through bonds magnetization transfer efficiency. We present here a robust structure-based assignment...
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08-14-2010 04:19 AM
HIFI-C: a robust and fast method for determining NMR couplings from adaptive 3D to 2D projections
HIFI-C: a robust and fast method for determining NMR couplings from adaptive 3D to 2D projections
Gabriel Cornilescu, Arash Bahrami, Marco Tonelli, John L. Markley and Hamid R. Eghbalnia
Journal of Biomolecular NMR; 2007; 38(4); pp 341-351
Abstract:
We describe a novel method for the robust, rapid, and reliable determination of J couplings in multi-dimensional NMR coupling data, including small couplings from larger proteins. The method, “High-resolution Iterative Frequency Identification of Couplings” (HIFI-C) is an extension of the adaptive and intelligent data collection approach...