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. 2017 Dec 8;1009:31–45. doi: 10.1007/978-981-10-6038-0_3

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© The Author(s) 2017

Open Access This chapter is licensed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license and indicate if changes were made.

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Fig. 3.5 — Stable mass heterogeneity. SEC-MALS/QELS analysis of a 185 kDa ATP binding protein reveal a leading shoulder in the QELS (magenta). The shoulder corresponded to a larger mass species by MALS (black line,lower left panel). To test if the protein was responsive to ATP, SEC-MALS/QELS was performed in the presence of 500 uM ATP-vanadate. The (+)ATP state showed a measurable and consistent decrease in radius-of-hydration (r_H) by QELS (cyan) indicating the protein undergoes as a significant conformational change. A small change in r_H would translate into an observable change by SAXS