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. 2010 Nov 2;21(4):410–425. doi: 10.1093/glycob/cwq173

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© The Author 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. For permissions, please e-mail: journals.permissions@oup.com.

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Fig. 8. — Binding kinetics of R5P (A) and the ATP analog (AMPPNP) (B) to Mt-PrsA using ITF spectroscopy. ITF spectroscopy was used to determine the binding properties of Mt-PrsA for its substrates R5P and ATP. Ligand-binding assays were carried out as described in the Materials and methods section. (A) A plot of ΔF_emission vs. [R5P] in the presence of no AMPPNP (filled squares) and 5 mM AMPPNP (filled circles) which was fitted to Eq. (7). (B) A plot of ΔF_emission vs. [AMPPNP] in the presence of no R5P (filled squares) and 5 mM R5P (filled circles) which was fitted to Eq. (9).