Literature DB >> 17593525

Model-free analysis for large proteins at high magnetic field strengths.

Shou-Lin Chang1, Andrew P Hinck, Rieko Ishima.   

Abstract

Protein backbone dynamics is often characterized using model-free analysis of three sets of (15)N relaxation data: longitudinal relaxation rate (R1), transverse relaxation rate (R2), and (15)N-{H} NOE values. Since the experimental data is limited, a simplified model-free spectral density function is often used that contains one Lorentzian describing overall rotational correlation but not one describing internal motion. The simplified spectral density function may be also used in estimating the overall rotational correlation time, by making the R2/R1 largely insensitive to internal motions, as well as used as one of the choices in the model selection protocol. However, such approximation may not be valid for analysis of relaxation data of large proteins recorded at high magnetic field strengths since the contribution to longitudinal relaxation from the Lorentzian describing the overall rotational diffusion of the molecule is comparably small relative to that describing internal motion. Here, we quantitatively estimate the errors introduced by the use of the simplified spectral density in model-free analysis for large proteins at high magnetic field strength.

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Year:  2007        PMID: 17593525     DOI: 10.1007/s10858-007-9171-9

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


  51 in total

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8.  An improved method for distinguishing between anisotropic tumbling and chemical exchange in analysis of 15N relaxation parameters.

Authors:  N H Pawley; C Wang; S Koide; L K Nicholson
Journal:  J Biomol NMR       Date:  2001-06       Impact factor: 2.835

9.  Overcoming solvent saturation-transfer artifacts in protein NMR at neutral pH. Application of pulsed field gradients in measurements of 1H-15N Overhauser effects.

Authors:  Y C Li; G T Montelione
Journal:  J Magn Reson B       Date:  1994-09

10.  Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.

Authors:  N A Farrow; R Muhandiram; A U Singer; S M Pascal; C M Kay; G Gish; S E Shoelson; T Pawson; J D Forman-Kay; L E Kay
Journal:  Biochemistry       Date:  1994-05-17       Impact factor: 3.162

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  1 in total

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