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....
Simple tests for the validation of multiple field spin relaxation data
Simple tests for the validation of multiple field spin relaxation data
Abstract 15N spin relaxation data is widely used to extract detailed dynamic information regarding bond vectors such as the amide Nâ??H bond of the protein backbone. Analysis is typically carried using the Lipariâ??Szabo model-free approach. Even though the original model-free equation can be determined from single field R 1, R 2 and NOE, over-determination of more complex motional models is dependent on the recording of multiple field datasets. This is especially important for the characterization of conformational...
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[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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[NMR paper] Spin-state-selective TPPI: a new method for suppression of heteronuclear coupling con
Spin-state-selective TPPI: a new method for suppression of heteronuclear coupling constants in multidimensional NMR experiments.
Related Articles Spin-state-selective TPPI: a new method for suppression of heteronuclear coupling constants in multidimensional NMR experiments.
J Magn Reson. 1999 Aug;139(2):443-6
Authors: Schulte-Herbrüggen T, Briand J, Meissner A, Sørensen OW
A novel multidimensional NMR pulse sequence tool, spin-state-selective time-proportional phase incrementation (S(3) TPPI), is introduced. It amounts to application of...
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[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...
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Self-diffusion in Polymer Systems studied by Magnetic Field-Gradient Spin-Echo NMR Me
Self-diffusion in Polymer Systems studied by Magnetic Field-Gradient Spin-Echo NMR Methods
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 13 April 2010</br>
Harald, Walderhaug , Olle, Söderman , Daniel, Topgaard</br>
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Computational Study andMolecular Orbital Analysisof NMR Shielding, Spin–Spin Coupling, and Electric Field Gradientsof Azido Platinum Complexes
Linear Mode
