Relaxation data in NMR is often used for dynamics analysis, by modeling motion in the sample with a correlation function consisting of one or more decaying exponential terms, each described by an order parameter, and correlation time. This method has its origins in the Lipari-Szabo model-free approach, which originally considered overall tumbling plus one internal motion and was later expanded to several internal motions. We consider several of these cases in the solid state, and find that if the real motion is more complex than the assumed model, then model fitting is biased towards correlation times where the relaxation data is most sensitive. This leads to unexpected distortions in the resulting dynamics description. We propose using dynamics detectors, which each characterize a range of correlation times, and can be used to give an analysis of protein motion without assuming a specific model of the correlation function.
[NMR paper] Structure-Function Analysis of the Non-Muscle Myosin Light Chain Kinase (nmMLCK) Isoform by NMR Spectroscopy and Molecular Modeling: Influence of MYLK Variants.
Structure-Function Analysis of the Non-Muscle Myosin Light Chain Kinase (nmMLCK) Isoform by NMR Spectroscopy and Molecular Modeling: Influence of MYLK Variants.
Related Articles Structure-Function Analysis of the Non-Muscle Myosin Light Chain Kinase (nmMLCK) Isoform by NMR Spectroscopy and Molecular Modeling: Influence of MYLK Variants.
PLoS One. 2015;10(6):e0130515
Authors: Shen K, Ramirez B, Mapes B, Shen GR, Gokhale V, Brown ME, Santarsiero B, Ishii Y, Dudek SM, Wang T, Garcia JG
Abstract
The MYLK gene encodes the...
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[NMR paper] Solution NMR analysis of the interaction between the actinoporin Sticholysin I and DHPC micelles. Correlation with backbone dynamics.
Solution NMR analysis of the interaction between the actinoporin Sticholysin I and DHPC micelles. Correlation with backbone dynamics.
Related Articles Solution NMR analysis of the interaction between the actinoporin Sticholysin I and DHPC micelles. Correlation with backbone dynamics.
Proteins. 2013 Nov 12;
Authors: Castilla AL, Santos FP, Schreier S, Pires JR
Abstract
Sticholysin I (StI), an actinoporin expressed as a water-soluble protein by the sea anemone Stichodactyla helianthus, binds to natural and model membranes, forming oligomeric...
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[NMR paper] The time correlation function perspective of NMR relaxation in proteins.
The time correlation function perspective of NMR relaxation in proteins.
The time correlation function perspective of NMR relaxation in proteins.
J Chem Phys. 2013 Aug 28;139(8):084107
Authors: Shapiro YE, Meirovitch E
Abstract
We applied over a decade ago the two-body coupled-rotator slowly relaxing local structure (SRLS) approach to NMR relaxation in proteins. One rotator is the globally moving protein and the other rotator is the locally moving probe (spin-bearing moiety, typically the (15)N-(1)H bond). So far we applied SRLS to...
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First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
Biochim Biophys Acta. 2011 Jan 25;
Authors: Pandit A, Morosinotto T, Reus M, Holzwarth AR, Bassi R, de Groot HJ
The light-harvesting complex II (LHCII) is the main component of the...
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[NMR paper] Determination of protein rotational correlation time from NMR relaxation data at vari
Determination of protein rotational correlation time from NMR relaxation data at various solvent viscosities.
Related Articles Determination of protein rotational correlation time from NMR relaxation data at various solvent viscosities.
J Biomol NMR. 2004 Dec;30(4):431-42
Authors: Korchuganov DS, Gagnidze IE, Tkach EN, Schulga AA, Kirpichnikov MP, Arseniev AS
An accurate determination of the overall rotation of a protein plays a crucial role in the investigation of its internal motions by NMR. In the present work, an innovative approach to the...
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[NMR paper] Automated analysis of large sets of heteronuclear correlation spectra in NMR-based dr
Automated analysis of large sets of heteronuclear correlation spectra in NMR-based drug discovery.
Related Articles Automated analysis of large sets of heteronuclear correlation spectra in NMR-based drug discovery.
J Med Chem. 2002 Dec 19;45(26):5649-54
Authors: Damberg CS, Orekhov VY, Billeter M
Drug discovery procedures based on NMR typically require the analysis of thousands of NMR spectra. For example, in "SAR by NMR", two-dimensional NMR spectra are recorded for a target protein mixed with ligand candidates from a comprehensive library of...
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[NMR paper] NMR analysis of the interaction between protein L and Ig light chains.
NMR analysis of the interaction between protein L and Ig light chains.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR analysis of the interaction between protein L and Ig light chains.
J Mol Biol. 1997 Jul 4;270(1):8-13
Authors: Enokizono J, Wikström M, Sjöbring U, Björck L, Forsén S, Arata Y, Kato K, Shimada I
Protein L is a cell wall protein expressed by some strains of the anaerobic bacterial species Peptostreptococcus magnus. It binds to immunoglobulin...
Because the light is better here: correlation-time analysis by NMR
Linear Mode
