TABLE 2.

Inhibition constants of native LDTI and the alkylated folding intermediates IIa^ALK and IIc^ALK. The equilibrium dissociation constant K_i of the complex with trypsin, the association and dissociation rate constants k_on and k_off, and the inactivation rate k_inact are given as mean ± S.D.

	Ki	kon	koff	kinact
	nm	m−1s−1	s−1	s−1
N	0.43 ± 0.05	7.1 ± 2.4·105	5.5 ± 0.5·10−4	3 ± 0.6·10−6
IIaALK	10.48 ± 0.97	2.4 ± 0.6·105	40.7 ± 9·10−4	38 ± 4·10−6
IIcALK	0.48 ± 0.09	10.0 ± 1.1·105	7.6 ± 1.6·10−4	30 ± 1·10−6