Rigorous analysis of static light scattering measurements on buffered protein solutions

Wills, Peter R. and Winzor, Donald J. (2017) Rigorous analysis of static light scattering measurements on buffered protein solutions. Biophysical Chemistry, 228 108-113. doi:10.1016/j.bpc.2017.07.007

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Author Wills, Peter R.
Winzor, Donald J.
Title Rigorous analysis of static light scattering measurements on buffered protein solutions
Journal name Biophysical Chemistry   Check publisher's open access policy
ISSN 1873-4200
0301-4622
Publication date 2017-09-01
Year available 2017
Sub-type Article (original research)
DOI 10.1016/j.bpc.2017.07.007
Open Access Status File (Author Post-print)
Volume 228
Start page 108
End page 113
Total pages 6
Place of publication Amsterdam, Netherlands
Publisher Elsevier BV
Language eng
Abstract Attention is drawn to the thermodynamic invalidity of the current practice of analyzing static light scattering measurements on globular proteins in terms of theory for a single solute because of its disregard of the need to consider small species such as buffer components as additional cosolutes rather than as part of the solvent. This practice continues despite its demonstrated inadequacy in studies of sucrose-supplemented protein solutions, where the aberrant behavior was recognized to be a consequence of physical protein interaction with the small cosolute. Failure to take into account the consequences of small cosolute effects renders extremely difficult any attempt to obtain a rigorous thermodynamic characterization of protein interactions by this empirical technique.
Keyword Protein–cosolute interactions
Static light scattering
Thermodynamic nonideality
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
 
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