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dc.contributor.authorAnggayasti, W.
dc.contributor.authorMancera, Ricardo
dc.contributor.authorBottomley, Steven
dc.contributor.authorHelmerhorst, Erik
dc.identifier.citationAnggayasti, W. and Mancera, R. and Bottomley, S. and Helmerhorst, E. 2016. Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions. Analytical Biochemistry. 499: pp. 43-50.

© 2016 Elsevier Inc. All rights reserved. Surface plasmon resonance (SPR) is a powerful technique for evaluating protein-protein interactions in real time. However, inappropriately optimized experiments can often lead to problems in the interpretation of data, leading to unreliable kinetic constants and binding models. Optimization of SPR experiments involving "sticky" proteins, or proteins that tend to aggregate, represents a typical scenario where it is important to minimize errors in the data and the kinetic analysis of those data. This is the case of High Mobility Group Box 1 and the receptor of advanced glycation end products. A number of improvements in protein purification, buffer composition, immobilization conditions, and the choice of flow rate are shown to result in substantial improvements in the accurate characterization of the interactions of these proteins and the derivation of the corresponding kinetic constants.

dc.titleOptimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions
dc.typeJournal Article
dcterms.source.titleAnalytical Biochemistry
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusFulltext not available

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