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. 2010 Sep 28;132(41):14577–14589. doi: 10.1021/ja105852y

Table 2. Changes in Conformational Entropy of Gal3C in Response to Ligand Bindinga.

state ΔSbb (J mol−1 K−1)b ΔSsc (J mol−1 K−1)c −TΔSconf (kJ/mol)d
lactose 187 ± 11 44 ± 6 −70 ± 4
L2−Gal3C 153 ± 9 35 ± 5 −57 ± 3
L3−Gal3C 185 ± 9 −7 ± 5 −54 ± 3
a

All entropies are relative to that for the apo state. Data include only those residues for which order parameters were determined in all four states (104 residues for the backbone and 50 residues for side chains).

b

Difference in backbone entropy obtained from experimental order parameters.

c

Difference in side-chain entropy obtained from experimental order parameters.

d

Contribution to the free energy of binding from conformational entropy obtained from experimental order parameters. T = 301 K.