Skip to main content
. Author manuscript; available in PMC: 2020 Jul 22.
Published in final edited form as: Eur Biophys J. 1991;19(3):125–140. doi: 10.1007/BF00185453

Table 1.

Anisotropy decays of single tryptophan proteins and peptides. obtained from global analysis with acrylamide quenching

Sample Θi (ps) r0 gi χR2
RNase T1a 6 520 0.310 1.76
2 110 0.022
7 140 0.290 1.45
S. Nucleaseb 9 890 0.303 1.99
91 0.018
10 160 0.301 0.97
Monellinc 3 750 0.282 44.0
360 0.073
6 000 0.240 1.57
ACTHd 625 0.260 85.3
200 0.189
1 800 0.119 2.00
Leu-try-leue 157 0.319 1.71
4 0.033
162 0.331 1.56
Gly-trp-glye 73 0.296 2.00
39 0.220
135 0.105 0.83
NATAe 56 0.323 1.06
Indole in MeOH, 40°C 12 0.290f 2.29
12 0.226g 2.20

Unless indicated otherwise, all measurements are in aqueous buffer at 20°C

a

100 mM Na acetate. pH 5.5

b

25 mM tris with 100 mM NaCl. pH = 7.0

c

100 mM Na acetate, pH = 3.6

d

10mM phosphate, pH =7

e

25 mM tris, pH =7.5

f

r0 was fixed at 0.29

g

r0 was a floating parameter