Literature DB >> 2363849

Surface fractality of proteins from theory and NMR data.

D Fushman1.   

Abstract

Different approaches to study protein surface fractality are considered. An approach based on analysis of surface versus molecular weight dependence is shown to be an informative tool for investigation of protein surface behaviour. An evidence for protein surface fractality, obtained with the use of this analysis from the data of both NMR measurements in protein solutions and computer analysis of protein structures, is presented. Obtained value of fractal dimension of protein surface (ds congruent to 2.2) is in a good agreement with the results of conventional approach (with variation of yardstick length) to protein surface fractality. A conclusion is made that surface enlargement due to the rise of protein molecular weight is accompanied by the increase of maximum scale of irregularities on protein surface. Possible effect of surface fractality on hydrodynamic characteristics of protein molecules in solution is discussed.

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Year:  1990        PMID: 2363849     DOI: 10.1080/07391102.1990.10508569

Source DB:  PubMed          Journal:  J Biomol Struct Dyn        ISSN: 0739-1102


  3 in total

1.  Self similarity of protein surfaces.

Authors:  T Goetze; J Brickmann
Journal:  Biophys J       Date:  1992-01       Impact factor: 4.033

2.  Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: Differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G.

Authors:  Jennifer B Hall; David Fushman
Journal:  J Biomol NMR       Date:  2003-11       Impact factor: 2.835

3.  Accessible surfaces of beta proteins increase with increasing protein molecular mass more rapidly than those of other proteins.

Authors:  Anna V Glyakina; Natalya S Bogatyreva; Oxana V Galzitskaya
Journal:  PLoS One       Date:  2011-12-01       Impact factor: 3.240

  3 in total

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