Literature DB >> 7850167

A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization.

J M Schurr1, H P Babcock, B S Fujimoto.   

Abstract

The effects of anisotropy of rotational diffusion and extent of dimerization on the performance of the simple and extended model-free formulas are investigated. Numerically exact 15N NMR R1, R2, and NOE data are simulated for cylindrically symmetric species and also for mixtures of spherical monomers and dimers with the same internal dynamics. The relevant internuclear vectors are assumed to move in isotropic deflection potentials fixed at different orientations in the molecule and to exhibit a single relaxation time in their internal correlation functions. The simple model-free formula is fitted to these simulated data in order to obtain the best-fit order parameter and internal relaxation time for each nucleus. Fitting is accomplished by the standard data-analysis protocol, in which a single common global correlation time is adjusted, and also by an alternative protocol, in which the global correlation time is adjusted separately for each nucleus. The extended model-free formula is likewise fitted to these same data. With noise-free data, the simple model-free formula and standard protocol yield remarkably good best-fit internal motion parameters up to moderate anisotropies (r = D parallel/D perpendicular = 2.0), but some or many of the NMR relaxation data are not fitted well even for quite modest anisotropies (r = 1.3). The extended model-free formula yields an improved fit to the NMR data, but predicts substantial amplitudes of nonexistent slow internal motions (tau approximately greater than 0.2 ns) for many of the nuclei for all r > or = 1.3. The simple model-free formula with the alternate protocol yields even better internal motion parameters than the standard protocol and also an excellent fit to the NMR relaxation data. The best-fit global correlation time for each nucleus corresponds very closely to the theoretical correlation time defined herein. Knowledge of these times would allow one not only to estimate the anisotropy of diffusion but also in favorable cases to infer the existence of slow internal motions. Inclusion of typical statistical errors in R1, R2, and NOE, or modest exchange contributions to R2, seriously degrades the performance of the simple model-free formula with either protocol, especially in regard to the internal relaxation times, which can exhibit very large deviations from their input value even for spherical diffusors. When the fraction of monomers existing as dimers lies in the range 0.1 < or = fd < or = 0.8, none of the three model-free approaches tested yields reliable internal motion parameters.

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Year:  1994        PMID: 7850167     DOI: 10.1006/jmrb.1994.1127

Source DB:  PubMed          Journal:  J Magn Reson B        ISSN: 1064-1866


  57 in total

1.  Flexibility of duplex DNA on the submicrosecond timescale.

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2.  Separating the contributions to 15N transverse relaxation in a fibronectin type III domain.

Authors:  A E Meekhof; S M Freund
Journal:  J Biomol NMR       Date:  1999-05       Impact factor: 2.835

3.  Solution structure and dynamics of GCN4 cognate DNA: NMR investigations.

Authors:  P Khandelwal; S C Panchal; P K Radha; R V Hosur
Journal:  Nucleic Acids Res       Date:  2001-01-15       Impact factor: 16.971

4.  Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data.

Authors:  P Dosset; J C Hus; M Blackledge; D Marion
Journal:  J Biomol NMR       Date:  2000-01       Impact factor: 2.835

5.  Comparison of the solution conformation and dynamics of antifreeze glycoproteins from Antarctic fish.

Authors:  A N Lane; L M Hays; N Tsvetkova; R E Feeney; L M Crowe; J H Crowe
Journal:  Biophys J       Date:  2000-06       Impact factor: 4.033

6.  Assessing potential bias in the determination of rotational correlation times of proteins by NMR relaxation.

Authors:  A L Lee; A J Wand
Journal:  J Biomol NMR       Date:  1999-02       Impact factor: 2.835

7.  Lipari-Szabo mapping: A graphical approach to Lipari-Szabo analysis of NMR relaxation data using reduced spectral density mapping.

Authors:  M Andrec; G T Montelione; R M Levy
Journal:  J Biomol NMR       Date:  2000-10       Impact factor: 2.835

8.  Overall rotational diffusion and internal mobility in domain II of protein G from Streptococcus determined from 15N relaxation data.

Authors:  M L Tillett; M J Blackledge; J P Derrick; L Y Lian; T J Norwood
Journal:  Protein Sci       Date:  2000-06       Impact factor: 6.725

9.  Key interactions in the immunoglobulin-like structure of apo-neocarzinostatin: evidence from nuclear magnetic resonance relaxation data and molecular dynamics simulations.

Authors:  N Izadi-Pruneyre; Y Blouquit; J Perez; P Minard; M Desmadril; J Mispelter
Journal:  Protein Sci       Date:  2001-11       Impact factor: 6.725

10.  Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin).

Authors:  Michael T Henzl; John J Tanner
Journal:  Protein Sci       Date:  2007-09       Impact factor: 6.725

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