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. Author manuscript; available in PMC: 2011 Jan 12.
Published in final edited form as: Biochemistry. 2010 Jan 12;49(1):236–246. doi: 10.1021/bi901725x

FIGURE 5. Effect of elimination of the inter-monomer salt bridge (Glu19 – Lys137) on the solution structure and Man-6-P binding affinity of sCD-MPR.

FIGURE 5

(A) Overlay of 1H-15N HSQC spectra collected on sCD-MPR in the presence (grey) and absence (magenta) of Man-6-P. The 1H-15N HSQC spectrum of EQKM (cyan) collected in the absence of Man-6-P is shown for comparison. The side chain amide group (Gln19) of EQKM is indicated by the dashed grey circle. (B) Apparent binding affinities (Kd) were obtained by 1H-15N HSQC spectroscopy titrating Man-6-P with 15N-labeled sCD-MPR or EQKM and monitoring chemical shift perturbations for three different nitrogen groups.