A method for rapid high-throughput biophysical analysis of proteins
Publication Date
2017-08-22Journal Title
Scientific Reports
ISSN
2045-2322
Publisher
Nature Publishing Group
Volume
7
Number
9071
Language
English
Type
Article
This Version
VoR
Metadata
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Itzhaki, L., & Perez Riba, A. (2017). A method for rapid high-throughput biophysical analysis of proteins. Scientific Reports, 7 (9071) https://doi.org/10.1038/s41598-017-08664-w
Abstract
Quantitative determination of protein thermodynamic stability is fundamental to many research areas, both basic and applied. Although chemical-induced denaturation is the gold-standard method, it has been replaced in many settings by semi-quantitative approaches such as thermal stability measurements. The reason for this shift is that chemical denaturation experiments are labour-intensive, sample-costly and time-consuming, and it has been assumed that miniaturisation to a high-throughput format would not be possible without concomitantly comprising data quality. Here we exploit current technologies to create a high-throughput label-free chemical denaturation method that is capable of generating replicate datasets on multiple proteins in parallel on a timescale that is at least ten times faster, much more economical on sample, and with the potential for superior data quality, than the conventional methods used in most research labs currently.
Keywords
assay systems, expression systems, thermodynamics
Sponsorship
Cancer Research UK (22676)
Embargo Lift Date
2100-01-01
Identifiers
External DOI: https://doi.org/10.1038/s41598-017-08664-w
This record's URL: https://www.repository.cam.ac.uk/handle/1810/267062
Rights
Attribution 4.0 International, Attribution 4.0 International, Attribution 4.0 International, Attribution 4.0 International, Attribution 4.0 International
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