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 exchange which affects R 2 in a field dependent manner. However, severe artifacts can be introduced if inconsistencies arise between experimental setups with different magnets (or samples). Here, we propose the use of simple tests as validation tools for the assessment of consistency between different datasets recorded at multiple magnetic fields. Synthetic data are used to show the effects of inconsistencies on the proposed tests. Moreover, an analysis of data currently deposited in the BMRB is performed. Finally, two cases from our laboratory are presented. These tests are implemented in the open-source program relax, and we propose their use as a routine check-up for assessment of multiple field dataset consistency prior to any analysis such as model-free calculations. We believe this will aid in the extraction of higher quality dynamics information from 15N spin relaxation data.
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....
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10-02-2011 08:25 AM
relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins
relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and μs motion of proteins
Abstract Investigation of protein dynamics on the ps-ns and μs-ms timeframes provides detailed insight into the mechanisms of enzymes and the binding properties of proteins. Nuclear magnetic resonance (NMR) is an excellent tool for studying protein dynamics at atomic resolution. Analysis of relaxation data using model-free analysis can be a tedious and time consuming process, which requires good knowledge of scripting procedures. The software relaxGUI was...
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06-06-2011 12:53 AM
relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and ?s motion of proteins.
relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and ?s motion of proteins.
relaxGUI: a new software for fast and simple NMR relaxation data analysis and calculation of ps-ns and ?s motion of proteins.
J Biomol NMR. 2011 May 27;
Authors: Bieri M, d'Auvergne EJ, Gooley PR
Investigation of protein dynamics on the ps-ns and ?s-ms timeframes provides detailed insight into the mechanisms of enzymes and the binding properties of proteins. Nuclear magnetic resonance (NMR) is an excellent tool for studying...
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05-28-2011 06:50 PM
Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins
Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 3 February 2011</br>
Monika, Bayrhuber , Roland, Riek</br>
Sensitivity enhancement in liquid state nuclear magnetic resonance (NMR) triple resonance experiments for the sequential assignment of proteins is important for the investigation of large proteins or protein complexes. We present here the 3D TROSY-MQ/CRINEPT-HN(CO)CA which makes...
[NMR paper] Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Related Articles Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
Proteins. 2005 Aug 15;60(3):367-81
Authors: van Dijk AD, Fushman D, Bonvin AM
When classical, Nuclear Overhauser Effect (NOE)-based approaches fail, it is possible, given high-resolution...
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12-01-2010 06:56 PM
[NMR paper] Relaxation-matrix formalism for rotating-frame spin-lattice proton NMR relaxation and
Relaxation-matrix formalism for rotating-frame spin-lattice proton NMR relaxation and magnetization transfer in the presence of an off-resonance irradiation field.
Related Articles Relaxation-matrix formalism for rotating-frame spin-lattice proton NMR relaxation and magnetization transfer in the presence of an off-resonance irradiation field.
J Magn Reson B. 1994 May;104(1):11-25
Authors: Kuwata K, Brooks D, Yang H, Schleich T
The derivation of a generalized relaxation matrix equation for the off-resonance rotating-frame spin-lattice...
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08-22-2010 03:33 AM
[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...
Simple tests for the validation of multiple field spin relaxation data
Linear Mode
