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. Author manuscript; available in PMC: 2010 Mar 1.
Published in final edited form as: Proteins. 2009 Mar;74(4):948–960. doi: 10.1002/prot.22203

Table 5.

Binding kinetics of combinations of point mutants, and cooperativity of the energetics.

Mutation1 kon, ×104 M−1s−1 koff, ×10−1 s−1 KD, μM ΔΔG, kcal/mol Coop2
WFTMT 1.98 0.0481 0.240 −1.28 ± 0.24 1.64
WFGMT 6.32 0.0135 0.0214 −2.72 ± 0.10 −0.56
1

Residue identities at positions 26, 27, 28, 51, and 100 on the TCRα chain. Mutant residues are in bold.

2

Cooperativity of the mutations, defined by ΔΔGmutant - Σ(ΔΔGindivdual point mutants)