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Open AccessArticle

The Use of Size Exclusion Chromatography to Monitor Protein Self-Assembly

Department of Drug Design, Structural Biology Unit, Groningen Research Institute of Pharmacy, University of Groningen, 9713AJ Groningen, The Netherlands
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Author to whom correspondence should be addressed.
Current address: HRTEM laboratory, Scientific and Technical Services, University of Oviedo-CINN, 33006 Oviedo, Spain.
Academic Editor: Albert Guskov
Crystals 2017, 7(11), 331; https://doi.org/10.3390/cryst7110331
Received: 6 September 2017 / Revised: 20 October 2017 / Accepted: 23 October 2017 / Published: 31 October 2017
(This article belongs to the Special Issue Recent Advances in Protein Crystallography)
High resolution size exclusion chromatography (SEC) coupled with static light scattering (SLS) analyses were conducted to study the effect of the mobile phase ionic strength and protein concentration on the output of SEC experiments. The results highlight the effect of small changes in the mobile phase composition on the estimation of molar masses estimated from retention time-based calibration curve compared with those obtained from SLS analysis. By comparing the SLS data with the SEC chromatograms, we show that SEC can provide helpful information on the protein aggregation state as macromolecules approach known precipitation points in their phase diagrams. This suggests the potential use of SEC as an easily accessible lab-based scanning methodology to monitor protein self-assembly prior to nucleation and crystallization. Implications for the use of SEC to study protein phase diagrams are discussed. View Full-Text
Keywords: size exclusion chromatography; static light scattering; protein aggregation; protein nucleation size exclusion chromatography; static light scattering; protein aggregation; protein nucleation
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MDPI and ACS Style

Adawy, A.; Groves, M.R. The Use of Size Exclusion Chromatography to Monitor Protein Self-Assembly. Crystals 2017, 7, 331.

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