Literature DB >> 26066679

Computing translational diffusion and sedimentation coefficients: an evaluation of experimental data and programs.

Mattia Rocco1, Olwyn Byron.   

Abstract

Hydrodynamic characterisation of (bio)macromolecules is a well-established field. Observables linked to translational friction, such as the translational diffusion (Dt(0)(20,w)) and sedimentation (s(0)(20,w)) coefficients, are the most commonly used parameters. Both can be computed starting from high-resolution structures, with several methods available. We present here a comprehensive study of the performance of public-domain software, comparing the calculated Dt(0)(20,w) and s(0)(20,w) for a set of high-resolution structures (ranging in mass from 12,358 to 465,557 Da) with their critically appraised literature experimental counterparts. The methods/programs examined are AtoB, SoMo, BEST, Zeno (all implemented within the US-SOMO software suite) and HYDROPRO. Clear trends emerge: while all programs can reproduce Dt(0)(20,w) on average to within ±5% (range -8 to +7%), SoMo and AtoB slightly overestimate it (average +2 and +1%, range -2 to +7 and -4 to +5%, respectively), and BEST and HYDROPRO underestimate it slightly more (average -3 and -4%, range -7 to +2 and -8 to +2%, respectively). Similar trends are observed with s(0)(20,w), but the comparison is likely affected by the necessary inclusion of the partial specific volume in the computations. The somewhat less than ideal performances could result from the hydration treatment in BEST and HYDROPRO, and the bead overlap removal in SoMo and AtoB. Interestingly, a combination of SoMo overlapping bead models followed by Zeno computation produced better results, with a 0% average error (range -4 to +4%). Indeed, this might become the method of choice, once computational speed considerations now favouring the 5 Å-grid US-SOMO AtoB approach are overcome.

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Year:  2015        PMID: 26066679     DOI: 10.1007/s00249-015-1042-9

Source DB:  PubMed          Journal:  Eur Biophys J        ISSN: 0175-7571            Impact factor:   1.733


  56 in total

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  6 in total

1.  Analytical ultracentrifugation (AUC): a seminal tool offering multiple solutions.

Authors:  Olwyn Byron; Ivo Nischang; Trushar R Patel
Journal:  Eur Biophys J       Date:  2018-10       Impact factor: 1.733

2.  GRPY: An Accurate Bead Method for Calculation of Hydrodynamic Properties of Rigid Biomacromolecules.

Authors:  Pawel J Zuk; Bogdan Cichocki; Piotr Szymczak
Journal:  Biophys J       Date:  2018-07-24       Impact factor: 4.033

3.  HullRad: Fast Calculations of Folded and Disordered Protein and Nucleic Acid Hydrodynamic Properties.

Authors:  Patrick J Fleming; Karen G Fleming
Journal:  Biophys J       Date:  2018-02-27       Impact factor: 4.033

4.  Recent advances in the UltraScan SOlution MOdeller (US-SOMO) hydrodynamic and small-angle scattering data analysis and simulation suite.

Authors:  Emre Brookes; Mattia Rocco
Journal:  Eur Biophys J       Date:  2018-03-28       Impact factor: 1.733

5.  A database of calculated solution parameters for the AlphaFold predicted protein structures.

Authors:  Emre Brookes; Mattia Rocco
Journal:  Sci Rep       Date:  2022-05-05       Impact factor: 4.996

6.  Disassembly of the self-assembled, double-ring structure of proteasome α7 homo-tetradecamer by α6.

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Journal:  Sci Rep       Date:  2015-12-14       Impact factor: 4.379

  6 in total

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