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Literature DB >> 8111234

Minimizing the effects of radio-frequency heating in multidimensional NMR experiments.

Abstract

Application of radio-frequency power in multidimensional NMR experiments can significantly increase the sample temperature compared to that of the surrounding gas flow. Radio-frequency heating effects become more severe at higher magnetic field strengths and ionic strengths. The effects are particularly noticeable for experiments that utilize 1H and/or 13C isotropic mixing and broadband decoupling. If radio-frequency power is applied during the systematically increasing evolution period t1, the sample temperature can change with t1 and thereby cause line-shape distortions. Such distortions are easily avoided by ensuring that the average radio-frequency power remains constant during the entire experiment.

Entities: Chemical

Mesh：

Substances：
Carbon Isotopes
Protons

Year: 1993 PMID： 8111234 DOI： 10.1007/bf00198374

Source DB: PubMed Journal: J Biomol NMR ISSN： 0925-2738 Impact factor: 2.835

2 in total

1. Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.

Authors: M Ikura; L E Kay; M Krinks; A Bax
Journal: Biochemistry Date: 1991-06-04 Impact factor: 3.162

2. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions.

Authors: M Piotto; V Saudek; V Sklenár
Journal: J Biomol NMR Date: 1992-11 Impact factor: 2.835

2 in total

27 in total

1. Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods.

Authors: J H Viles; B M Duggan; E Zaborowski; S Schwarzinger; J J Huntley; G J Kroon; H J Dyson; P E Wright
Journal: J Biomol NMR Date: 2001-09 Impact factor: 2.835

2. Rotational diffusion tensor of nucleic acids from 13C NMR relaxation.

Authors: Jerome Boisbouvier; Zhengrong Wu; Arika Ono; Masatsune Kainosho; Ad Bax
Journal: J Biomol NMR Date: 2003-10 Impact factor: 2.835

3. Direct determination of the heteronuclear T1/T2 ratio by off-resonance steady-state magnetization measurement: Investigation of the possible application to fast exchange characterization of 15N-labeled proteins.

Authors: M Guenneugues; P Berthault; H Desvaux; M Goldman
Journal: J Biomol NMR Date: 1999-12 Impact factor: 2.835

4. (13)CHD2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.

Authors: Enrico Rennella; Rui Huang; Algirdas Velyvis; Lewis E Kay
Journal: J Biomol NMR Date: 2015-08-14 Impact factor: 2.835

9. Refocusing revisited: an optimized, gradient-enhanced refocused HSQC and its applications in 2D and 3D NMR and in deuterium exchange experiments.

Authors: J H Davis
Journal: J Biomol NMR Date: 1995-06 Impact factor: 2.835

10. Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r).

Authors: Renee Otten; Janice Villali; Dorothee Kern; Frans A A Mulder
Journal: J Am Chem Soc Date: 2010-11-08 Impact factor: 15.419

Minimizing the effects of radio-frequency heating in multidimensional NMR experiments.

1. Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.

2. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions.

1. Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods.

2. Rotational diffusion tensor of nucleic acids from 13C NMR relaxation.

3. Direct determination of the heteronuclear T1/T2 ratio by off-resonance steady-state magnetization measurement: Investigation of the possible application to fast exchange characterization of 15N-labeled proteins.

4. (13)CHD2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.

5. Molecular Mechanism of the Pin1-Histone H1 Interaction.

6. Enhanced accuracy of kinetic information from CT-CPMG experiments by transverse rotating-frame spectroscopy.

7. MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.

8. Practical considerations for investigation of protein conformational dynamics by ¹⁵N R _1ρ relaxation dispersion.

9. Refocusing revisited: an optimized, gradient-enhanced refocused HSQC and its applications in 2D and 3D NMR and in deuterium exchange experiments.

10. Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r).