. Author manuscript; available in PMC: 2017 Jun 2.

Published in final edited form as: Biochemistry. 2011 Mar 10;50(13):2575–2584. doi: 10.1021/bi101116a

Table 2.

Comparison of dissociation constants for the binding interaction between WW domain peptides and ssDNA and dsDNA sequences and Polyproline Helix^a

Peptide	ssDNA K_d, µM (error)	dsDNA K_d, µM (error)	Polyproline Helix K_d, µM (error)
Native FBP11 WW1 domain	>6000^b	>500^b	60 (6)
WKWK dimer	3.5 (0.2)^c	4.6 (0.4)^c	n. d.^d
TAMRA-Mut1	20 (4)	190 (20)	No binding observed

^(a)

Conditions: 10 mM sodium phosphate buffer, 100 mM NaCl, pH 7.0, 25 °C. Each value is the average of at least two measurements. The error is from the fitting. n.d. denotes a measurement that was not determined.

^(b)

This data was collected using fluorescence anisotropy with Bodipy-labeled DNA.

^(c)

These values were reported previously.^5–6

^(d)

n. d. = not determined.