Chemistry World A new spin on protein NMR Chemistry World
The researchers have described a new technique for rapidly obtaining solid samples of protein for nuclear magnetic resonance interrogation without needing to crystallise the protein. The method, which combines solid-state NMR with ultracentrifugation, ...
Water proton spin saturation affects measured protein backboneN spin relaxation rates
Water proton spin saturation affects measured protein backboneN spin relaxation rates
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 1 October 2011</br>
Kang*Chen, Nico*Tjandra</br>
Protein backboneN NMR spin relaxation rates are useful in characterizing the protein dynamics and structures. To observe the protein nuclear-spin resonances a pulse sequence has to include a water suppression scheme. There are two commonly employed methods, saturating or dephasing the water spins with pulse field gradients and keeping them unperturbed with flip-back pulses....
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Angew Chem Int Ed Engl. 2011 Mar 18;
Authors: Salmon L, Ortega Roldan JL, Lescop E, Licinio A, van Nuland N, Jensen MR, Blackledge M
[NMR paper] Investigation of the NMR spin-spin coupling constants across the hydrogen bonds in ub
Investigation of the NMR spin-spin coupling constants across the hydrogen bonds in ubiquitin: the nature of the hydrogen bond as reflected by the coupling mechanism.
Related Articles Investigation of the NMR spin-spin coupling constants across the hydrogen bonds in ubiquitin: the nature of the hydrogen bond as reflected by the coupling mechanism.
J Am Chem Soc. 2004 Apr 28;126(16):5093-107
Authors: Tuttle T, Kraka E, Wu A, Cremer D
The indirect scalar NMR spin-spin coupling constants across the H-bonds of the protein ubiquitin were calculated,...
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Studies probe key flu protein - Chemistry World
Studies probe key flu protein - Chemistry World
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Studies probe key flu protein
Chemistry World
Both studies, published back-to-back in Science, use solid-state nuclear magnetic resonance to probe the fine structure of the M2 channel protein and ...
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10-21-2010 07:11 PM
[NMR paper] 19F-NMR spin-spin relaxation (T2) method for characterizing volatile anesthetic bindi
19F-NMR spin-spin relaxation (T2) method for characterizing volatile anesthetic binding to proteins. Analysis of isoflurane binding to serum albumin.
Related Articles 19F-NMR spin-spin relaxation (T2) method for characterizing volatile anesthetic binding to proteins. Analysis of isoflurane binding to serum albumin.
Biochemistry. 1992 Aug 11;31(31):7069-76
Authors: Dubois BW, Evers AS
This paper characterizes the low-affinity ligand binding interactions of a fluorinated volatile anesthetic, isoflurane (CHF2OCHClCF3), with bovine serum albumin...
A new spin on protein NMR - Chemistry World
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