Table 2.

Wild type and variant lysozymes kinetic folding phases

		Wild type	R6,127-Cxa	SS30–115	SS64–80	SS76–94
Tryp Fluo	burst	100 ± 5	90	45 ± 3	100 ± 6	100 ± 4
	k1	80 ± 10	>5	9 ± 1	85 ± 9	81 ± 11
	k2	3 ± 1	n.o.	n.o.	11 ± 1.5	0.7 ± 0.1
ANS Fluo	burst	100 ± 9	n.s.	100 ± 8	105 ± 10	80 ± 7
	k1	38 ± 13	n.s.	6 ± 1.5	17 ± 9	58 ± 10
	k2	3 ± 1	n.s.	n.o.	4 ± 0.8	0.6 ± 0.2
Θ228 nm	burst	100 ± 3	100	100 ± 4	100 ± 6	100 ± 5
	k1	37 ± 12 (62 ± 11)b	n.o.	n.o.	n.d.	n.o.
	k2	3 ± 1	n.o.	n.o.	n.d.	n.o.

The amplitudes of the burst of tryptophan fluorescence (Tryp Fluo), bound ANS fluorescence (ANS Fluo), and ellipticity at 228 nm (Θ_{228 nm}) are expressed in percent of the difference between the signals observed for the protein in 6 M GuHCl and for natural lysozyme during the flow phase (i.e., for the burst intermediate). k1 is the rate constant determined for the rapid (or unique) phase observed after the burst; k2 is that determined for the slow phase. Both are expressed in seconds⁻¹; n.o., not observed; n.d., the rate constant could not be determined; n.s., the corresponding signal was not studied.

^a Estimated from published results (Denton et al. 1994; Eyles et al. 1994).

^b The value obtained in these experiments was underestimated (see text). The value in parentheses is the more precise one obtained under the same experimental conditions (Chaffotte et al. 1992).