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. Author manuscript; available in PMC: 2011 May 4.
Published in final edited form as: Biochemistry. 2010 May 4;49(17):3555–3566. doi: 10.1021/bi100069s

Table 1.

ITC binding data for the interaction of χ and PriA with E.coli SSB C-terminal peptides in different solution conditions*.

χ
P15		 χ
P9		 χ
WP9		 PriA
P15		 PriA
P9		 PriA
WP9
Buffer T,
pH 7.5, 25°C
20 mM NaCl 		n=0.88±0.04
K=(0.8±0.1)×106
ΔH= −7.7±0.4		 n=0.92±0.04
K=(0.8±0.1)×106
ΔH= −8.2±0.4		 _ n=1.03±0.06
K=(1.6±0.4)×106
ΔH= −7.0±0.5		 n=0.89±0.05
K=(2.0±0.3)×106
ΔH= −6.7±0.3		 _
Buffer C,
pH 7.0, 25°C
20 mM NaCl 		n=0.91±0.02
K=(1.5±0.2)×106
ΔH= −9.5±0.3		 n=1.0±0.1
K=(1.6±0.4)×106
ΔH= −7.9±0.4		 n=1.02±0.03
K=(1.2±0.1)×106
ΔH= −8.0±0.3		 n=0.90±0.02
K=(2.7±0.2)×106
ΔH= −20.7±0.8		 _ n=0.95±0.02
K=(1.6±0.2)×106
ΔH= −14.5±0.5
Buffer C,
pH 7.0, 25°C
200 mM NaCl 		_ _ n=0.96±0.03
K=(3.0±0.2)×105
ΔH= −9.2±0.4		 n=0.92±0.03
K=(3.6±0.2)×105
ΔH= −14.0±0.6		 n=0.81±0.12
K=(1.8±0.6)×105
ΔH= −17.3.0±0.6		 n=1.1±0.1
K=(2.3±0.3)×105
ΔH= −13.0±1.3
*

binding parameters: n – stoichiometry of binding, K (M−1) – observed association equilibrium constant, ΔH (kcal/mol) – enthalpy change