Related ArticlesImproved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
J Biomol NMR. 1991 Nov;1(4):447-56
Authors: Güntert P, Wüthrich K
A new strategy for NMR structure calculations of proteins with the variable target function method (Braun, W. and Go, N. (1985) J. Mol. Biol., 186, 611) is described, which makes use of redundant dihedral angle constraints (REDAC) derived from preliminary calculations of the complete structure. The REDAC approach reduces the computation time for obtaining a group of acceptable conformers with the program DIANA 5-100-fold, depending on the complexity of the protein structure, and retains good sampling of conformation space.
Al NMR: a novel NMR data processing program optimized for sparse sampling
Al NMR: a novel NMR data processing program optimized for sparse sampling
Abstract Sparse sampling in biomolecular multidimensional NMR offers increased acquisition speed and resolution and, if appropriate conditions are met, an increase in sensitivity. Sparse sampling of indirectly detected time domains combined with the direct truly multidimensional Fourier transform has elicited particular attention because of the ability to generate a final spectrum amenable to traditional analysis techniques. A number of sparse sampling schemes have been described including radial sampling, random...
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11-17-2011 01:47 AM
High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data
High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data
Abstract X-ray diffraction and nuclear magnetic resonance spectroscopy (NMR) are the staple methods for revealing atomic structures of proteins. Since crystals of biomolecular assemblies and membrane proteins often diffract weakly and such large systems encroach upon the molecular tumbling limit of solution NMR, new methods are essential to extend structures of such systems to high resolution. Here we present a method that incorporates solid-state NMR restraints alongside...
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09-26-2011 06:42 AM
High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data.
High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data.
High-resolution membrane protein structure by joint calculations with solid-state NMR and X-ray experimental data.
J Biomol NMR. 2011 Sep 22;
Authors: Tang M, Sperling LJ, Berthold DA, Schwieters CD, Nesbitt AE, Nieuwkoop AJ, Gennis RB, Rienstra CM
Abstract
X-ray diffraction and nuclear magnetic resonance spectroscopy (NMR) are the staple methods for revealing atomic structures of proteins. Since crystals of biomolecular...
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09-23-2011 05:30 PM
[Question from NMRWiki Q&A forum] Exporting integral data for use in calculations
Exporting integral data for use in calculations
Hello people,
For my internship I am attempting to fully automate monomer composition analysis on Bruker TOPSPIN 2.0 using visual basic and macro's. It's almost fully functional but I've come across the following problem:
I want to use the integral data of a spectrum in calculations (i.e. export them to an excel template) but so far I've found no way of exporting integral data without using the mouse (I can make visual basic simulate mouse clicks, but it's not a method I like using since it makes the program very prone to failure or...
nmrlearner
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11-22-2010 07:08 PM
[NMR paper] Refinement of the protein backbone angle psi in NMR structure calculations.
Refinement of the protein backbone angle psi in NMR structure calculations.
Related Articles Refinement of the protein backbone angle psi in NMR structure calculations.
J Biomol NMR. 2000 Jan;16(1):47-58
Authors: Sprangers R, Bottomley MJ, Linge JP, Schultz J, Nilges M, Sattler M
Cross-correlated relaxation rates involving the Calpha-Halpha dipolar interaction and the carbonyl (C') chemical shift anisotropy (CSA) have been measured using two complementary 3D experiments. We show that the protein backbone angle psi can be directly refined...
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11-18-2010 09:15 PM
[Question from NMRWiki Q&A forum] Free program to calculate the theoretical second moment from crystal structure data?
Free program to calculate the theoretical second moment from crystal structure data?
Does anyone know of a free, available program I can use to calculate the theoretical second moment from crystal structure data? I was only able to find one online, written in a mix of FORTRAN 77/90. The current limitations of the program can't accommodate my system (big unit cell and lots of atoms), and FORTRAN coding really isn't my fortay.
Ideally, the program would be able to simulate second moment(s) by defining specific rotational axes, and modeling different rotational rates and hopping angles...
nmrlearner
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09-29-2010 10:24 AM
[NMR paper] Relaxation data in NMR structure determination: model calculations for the lysozyme-G
Relaxation data in NMR structure determination: model calculations for the lysozyme-Gd3+ complex.
Related Articles Relaxation data in NMR structure determination: model calculations for the lysozyme-Gd3+ complex.
Proteins. 1991;10(2):117-29
Authors: Sutcliffe MJ, Dobson CM
The effect of including paramagnetic relaxation data as additional restraints in the determination of protein tertiary structures from NMR data has been explored by a systematic series of model calculations. The system used for testing the method was the 2.0 A resolution...
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08-21-2010 11:16 PM
[NMR paper] Improved efficiency of protein structure calculations from NMR data using the program
Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
Related Articles Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
J Biomol NMR. 1991 Nov;1(4):447-56
Authors: Güntert P, Wüthrich K
A new strategy for NMR structure calculations of proteins with the variable target function method (Braun, W. and Go, N. (1985) J. Mol. Biol., 186, 611) is described, which makes use of...
Improved efficiency of protein structure calculations from NMR data using the program
Linear Mode
