[NMR paper] Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.
Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.
Related Articles Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.
J Biomol NMR. 2014 Aug 17;
Authors: Esadze A, Zandarashvili L, Iwahara J
Abstract
Recent studies have shown that lysine side-chain NH3 (+) groups are excellent probes for NMR investigations of dynamics involving...
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08-19-2014 11:21 AM
[NMR paper] Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements.
Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements.
Related Articles Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements.
Protein Expr Purif. 2014 Mar 21;
Authors: Kroupa T, Prchal J, Doležal M, Ruml T, Hrabal R
Abstract
Nuclear magnetic resonance (NMR) is a powerful technique for solving protein structures orstudying their interactions. However, it requires molecules labeled with NMR sensitive isotopes like carbon(13)C and...
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03-26-2014 12:44 PM
Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements
Cost-effective method for the preparation of uniformly labeled myristoylated proteins for NMR measurements
Publication date: Available online 21 March 2014
Source:Protein Expression and Purification</br>
Author(s): Tomáš Kroupa , Jan Prchal , Michal Doležal , Tomáš Ruml , Richard Hrabal</br>
Nuclear magnetic resonance (NMR) is a powerful technique for solving protein structures orstudying their interactions. However, it requires molecules labeled with NMR sensitive isotopes like carbon13C and nitrogen15N. The recombinant expression of labeled proteins is simple...
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03-22-2014 01:28 AM
A cost-effective look at proteins - with a little help from robotics - Cordis News
http://www.bionmr.com//t3.gstatic.com/images?q=tbn:ANd9GcTypMhbcsoTBmkGzm1ZmzjTHj-b-AsNVL4y8L03Y0oBfj2cCZUDv2gZmGEzmim-0VUKjKStcwU
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A cost-effective look at proteins - with a little help from robotics
Cordis News
Until now, a number of methods have been used to study static protein structures, including X-ray crystallography and nuclear magnetic resonance. However, these methods are of no use for proteins that are on the move; analytical methods, computer ...
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A cost-effective look at proteins - with a little help from...
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09-14-2013 01:46 AM
Scientists find new source of versatility so 'floppy' proteins can get things done - EurekAlert (press release)
Scientists find new source of versatility so 'floppy' proteins can get things done - EurekAlert (press release)
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Scientists find new source of versatility so 'floppy' proteins can get things done
EurekAlert (press release)
But IDPs don't connect willy-nilly with other proteins, and scientists have wondered how they regulate their diverse interactions. Wright's laboratory and others have been studying these interactions using a technique called nuclear magnetic resonance ...
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06-21-2013 12:16 AM
ncIDP-assign: A SPARKY extension for the effective NMR assignment of intrinsically disordered proteins.
ncIDP-assign: A SPARKY extension for the effective NMR assignment of intrinsically disordered proteins.
ncIDP-assign: A SPARKY extension for the effective NMR assignment of intrinsically disordered proteins.
Bioinformatics. 2011 Mar 3;
Authors: Tamiola K, Mulder FA
SUMMARY: We describe here the ncIDP-assign extension for the popular NMR assignment programme SPARKY, which aids in the sequence-specific resonance assignment of intrinsically disordered proteins (IDPs). The assignment plugin greatly facilitates the effective matching of a set of...
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03-05-2011 01:02 PM
[NMR paper] Effective rotational correlation times of proteins from NMR relaxation interference.
Effective rotational correlation times of proteins from NMR relaxation interference.
Related Articles Effective rotational correlation times of proteins from NMR relaxation interference.
J Magn Reson. 2006 Jan;178(1):72-6
Authors: Lee D, Hilty C, Wider G, Wüthrich K
Knowledge of the effective rotational correlation times, tauc, for the modulation of anisotropic spin-spin interactions in macromolecules subject to Brownian motion in solution is of key interest for the practice of NMR spectroscopy in structural biology. The value of tauc enables...
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12-01-2010 06:56 PM
[NMR paper] A simple and effective NMR cell for studies of encapsulated proteins dissolved in low
A simple and effective NMR cell for studies of encapsulated proteins dissolved in low viscosity solvents.
Related Articles A simple and effective NMR cell for studies of encapsulated proteins dissolved in low viscosity solvents.
J Biomol NMR. 2002 Aug;23(4):311-6
Authors: Flynn PF, Milton MJ, Babu CR, Wand AJ
Application of triple-resonance and isotope-edited-NOE methods to the study of increasingly larger macromolecules and their complexes remains a central goal of solution NMR spectroscopy. The slow reorientational motion of larger molecules...
Floppy but fast: Spaghetti-like proteins are surprisingly effective 'keys' - Phys.Org
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