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. Author manuscript; available in PMC: 2013 Apr 4.
Published in final edited form as: J Biol Chem. 2007 Nov 8;283(3):1401–1410. doi: 10.1074/jbc.M703831200

TABLE 1.

Dissociation constants (μM) for Binding CaM to PEP-19, PEP(28–62), and PEP(39–62)

Assay PEP-19 PEP(28–62) PEP(39–62)
Kd1 Kd2
NMRa 29 ± 0.7 24 ± 0.8 b
Fluorescencec 18 ± 3 NDd 0.24 ± 0.04
FRET 20 ± 4 ND 0.16 ± 0.05 27 ± 3
a

Values are the average mean ± S.E. of Kd values derived separately from chemical shift changes for 1H and/or 15N nuclei of amides for residues 99, 105, 109, 116, 117, 146, and 147.

b

NMR data fit poorly to either single or two-site binding models. Fluorescence data fit best to a single-site binding model.

c

The values derived from fluorescence and FRET data are the mean ± S.E. of three to four experiments.

d

ND, not determined.