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Probing the Average Local Structures of Biomolecules Using Small-angle Scattering and Scaling Laws
Published
Author(s)
Max NMN Watson, Joseph E. Curtis
Abstract
Small-angle neutron and X-ray scattering have become invaluable tools for probing the nanos- tructure of molecules in solution. It was recently shown that the definite integral of the scattering profile exhibits a scaling (power-law) behavior with respect to molecular mass. We derive the origin of this relationship. While the behavior does not follow a single scaling law over all molecular sizes, we discuss how an apparent scaling relationship can be used to identify differing levels of disorder over `local¿ {approximatelay less than}30 A distances. We apply our analysis to globular and intrinsically disordered proteins.
, M.
and Curtis, J.
(2014),
Probing the Average Local Structures of Biomolecules Using Small-angle Scattering and Scaling Laws, Biophysical Journal, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=914771
(Accessed October 8, 2025)