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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

Table 1.

Thermodynamic parameters describing allostery in AAC(6′)-Ii

KA1 (×104 M−1)a 2.1 ±0.1
KA2 (×104 M−1)b 2.8 ±0.1
KU0c 0.20 ±0.06
KU1d 0.38 ±0.07
ΔGA1 (kcal mol−1)e −6.13 ±0.03
ΔGA2 (kcal mol−1)f −6.32 ±0.02
ΔGU0 (kcal mol−1)g 1.0 ±0.2
ΔGU1 (kcal mol−1)h 0.6 ±0.1
ΔHA1 (kcal mol−1)i −22.9 ±0.8
ΔHA2 (kcal mol−1)j −28.1 ±0.8
ΔHU0 (kcal mol−1)k −71 ±7
ΔHU1 (kcal mol−1)l −93 ±6
ΔCp,A1 (cal mol−1 K−1)m −790 ±40
ΔCp,A2 (cal mol−1 K−1)n −820 ±30
ΔCp,U0 (cal mol−1 K−1)o 2100 NA
ΔCp,U1 (cal mol−1 K−1)o 2100 NA
[] ′F (deg cm2 dmol−1)p −7600 ±200
[] ′U (deg cm2 dmol−1)q −4040 ±20
mF (deg cm2 dmol−1 K−1)r 54 ±3
mU (deg cm2 dmol−1 K−1)s 8 ±2

T′=37°C

a

Equilibrium association constant for the native (non-melted) enzyme and the first AcCoA molecule at T′

b

Equilibrium association constant for the native (non-melted) enzyme and the second AcCoA molecule at T′

c

Equilibrium constant for subunit melting in the 0-bound enzyme at T′

d

Equilibrium constant for melting of the unbound subunit in the 1-bound enzyme at T′

e

Free energy change upon binding of one molecule of AcCoA to the native (non-melted) 0-bound enzyme at T′

f

Free energy change upon binding of one molecule of AcCoA to the native (non-melted) 1-bound enzyme at T′

g

Free energy change upon melting of a single subunit in the 0-bound enzyme at T′

h

Free energy change upon melting of the unbound subunit in the 1-bound enzyme at T′

i

Enthalpy change upon binding of one molecule of AcCoA to the native (non-melted) 0-bound enzyme at T′

j

Enthalpy change upon binding of one molecule of AcCoA to the native (non-melted) 1-bound enzyme at T′

k

Enthalpy change upon melting of a single subunit in the 0-bound enzyme at T′

l

Enthalpy change upon melting of the unbound subunit in the 1-bound enzyme at T′

m

Heat capacity change upon binding of one molecule of AcCoA to the native (non-melted) 0-bound enzyme

n

Heat capacity change upon binding of one molecule of AcCoA to the native (non-melted) 1-bound enzyme

o

Heat capacity change upon subunit melting. These values were fixed at the value obtained for a monomeric mutant of AAC(6′)-Ii

p

CD molar ellipticity of a native (non-melted) subunit at T′

q

CD molar ellipticity of a melted subunit at T′

r

Temperature dependence of the molar ellipticity of a native subunit

s

Temperature dependence of the molar ellipticity of a melted subunit