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. Author manuscript; available in PMC: 2012 Jan 20.
Published in final edited form as: Nat Struct Mol Biol. 2011 Jan 30;18(3):288–294. doi: 10.1038/nsmb.1978

Figure 4.

Figure 4

Analysis of NMR titration data. (a) Fraction of the enzyme in the 0-bound, 1-bound, and 2-bound states determined by ITC. (b) Intensities of the apo (dashed line) and holo (solid line) peaks for Leu56 as a function of [AcCoA]. The intensities were analyzed to extract the relative contribution of the 1-bound enzyme to the signals (I1apo,holo) as described in the text. The lines correspond to the optimized theoretical intensities. (c) Histograms of the relative contribution of the 1-bound enzyme to apo (I1apo) and holo (I1holo) peaks in titrations of AAC(6′)-Ii with AcCoA.