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Molecular weight–gyration radius relation of globular proteins: a comparison of light scattering, small‐angle X‐ray scattering and structure‐based data
Author(s) -
Smilgies DetlefM.,
FoltaStogniew Ewa
Publication year - 2015
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s1600576715015551
Subject(s) - radius of gyration , scattering , globular protein , small angle scattering , globular cluster , gyration , exponent , radius , small angle x ray scattering , power law , biological small angle scattering , physics , crystallography , molecular physics , chemistry , small angle neutron scattering , polymer , optics , geometry , stars , astrophysics , nuclear magnetic resonance , neutron scattering , mathematics , statistics , linguistics , computer science , philosophy , computer security
The molecular weight–gyration radius relation for a number of globular proteins based on experimental light scattering data is compared with small‐angle X‐ray scattering data recently published by Mylonas & Svergun [ J. Appl. Cryst. (2007), 40 , s245–s249]. In addition, other recent experimental data and theoretical calculations are reviewed. It is found that the M W – R g relation for the globular proteins is well represented by a power law with an exponent of 0.37 (2).
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