Table 2.

Parameters obtained from the fit with SG distributions and CBX model

Solvent	Peptide	SG distributions			CBX model
		A	B	D (10−6 cm2 s−1cP)	dα (Å)	ΔkR (%)	ΔE (%)	〈r2〉1/2 (Å)	nS	D (10−6 cm2 s−1cP)
Water	agq	10	11	1.0 ± 0.1	2.2	5	7	19.8	1.76	1.2 ± 0.2
	age	9	12	1.8 ± 0.4	3.0	1	10	20.3	1.85	2.2 ± 0.5
	aqe	11	16	1.1 ± 0.2	5.0	1	0	22.6	2.52	1.1 ± 0.2
Urea	agq	11	14	1.6 ± 0.2	4.2	0	1	21.1	1.91	1.5 ± 0.3
	age	12	14	2.0 ± 0.2	4.3	3	7	21.2	1.93	1.6 ± 0.2
	aqe	11	18	1.3 ± 0.1	5.4	3	6	24.4	2.68	1.1 ± 0.2
GdmCl	agq	12	13	0.78 ± 0.1	3.7	2	4	20.7	1.93	0.75 ± 0.1
	age	10	16	1.2 ± 0.2	5.1	4	1	22.0	2.12	1.1 ± 0.2
	aqe	12	17	0.37 ± 0.1	5.2	4	3	23.0	3.05	0.35 ± 0.1

Tryptophan-cysteine distance distributions obtained as skewed Gaussians, where p(r) ∝ r²exp[−(r-B)²/A²], and from the CBX model are extracted minimizing the sum of squared differences calculated through Eq. 5 between the measured and the computed values of k_R and 〈E〉. Intrachain diffusion coefficients D are extracted from the Eq. 6 using the selected p(r) and the measured ηk_D+. For each distance distribution simulated with the CBX model the table reports the value of the hard sphere diameter d_α, the percental errors Δk_R and ΔE between measured and computed values of k_R and 〈E〉 respectively, the computed rms tryptophan-cysteine distance and the average chain correlation length, n_S, in units of number of orientationally correlated residues (see Materials and Methods).