Role of Molecular Flexibility and Colloidal Descriptions of Proteins in Crowded Environments from Small-Angle Scattering

Published

November 10, 2016

Author(s)

Maria Monica Castellanos Mantilla, Nicholas J. Clark, Max C. Watson, Susan Krueger, Arnold McAuley, Joseph Curtis

Abstract

Small-angle scattering is a powerful technique to study molecular conformation and interactions in a variety of systems. Recent work has questioned the validity of analyzing small-angle scattering data of protein solutions with models from the colloidal chemistry field, because proteins are flexible molecules that can sample a large configurational space. We have investigated the role of multiple protein configurations on the effective structure factor from small-angle scattering, S'(Q), which contains information about protein-protein interactions in crowded environments. Our results elucidate the role that molecular shape has on S'(Q) in globular and flexible proteins. Although both shape anisotropy and flexibility have a non-negligible effect on S'(Q), we find that colloidal models can be useful to describe inter-particle correlations in proteins at certain length scales. We provide tools to estimate the validity of these models and calculate a range of theoretical parameters that encompass ensembles of structures.

Citation

Journal of Physical Chemistry B

Volume

120

Issue

49

Pub Type

Journals

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Keywords

protein crowding, small-angle scattering, colloidal models, protein-protein interactions, protein structure

Citation

, M. , , N. , , M. , Krueger, S. , McAuley, A. and , J. (2016), Role of Molecular Flexibility and Colloidal Descriptions of Proteins in Crowded Environments from Small-Angle Scattering, Journal of Physical Chemistry B, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=920592 (Accessed April 25, 2024)