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. Author manuscript; available in PMC: 2012 Aug 1.
Published in final edited form as: Biopolymers. 2011 Mar 25;95(8):550–558. doi: 10.1002/bip.21628

Table 1.

Comparisons of Rg from continuous-flow SAXS.a

Proteinb SAXS Rgc Dead time
Unfolded (Å) Continuous-flow burst phase (Å) Native (Å)
Ub42 26 25.93 ± 0.03 13.9 2.5 ms
ctAcP42 31 28.41 ± 0.23 14.6 2.5 ms
DHFR30 30.7 23.2 ± 0.3 16.6 ± 0.1 300 μs
αTS31 43 34 18.1 150 μs
cyt c26 24 20.5 ± 1 13.9 160 μs
apoMb51 29.7 ± 1.7 23.7 ± 0.9 18.2 ± 0.2 300 μs
SMN53 25.5 ± 0.5 18.2 ± 0.4 15.8 ± 0.2 300 μs
HO52 37.8 ± 1.2 26.1 ± 1.1 23 ± 1.2 600 μs
a

Radii of gyration of the burst-phases of different proteins observed by continuous-flow refolding kinetics. The sizes of the native and unfolded states are also given for reference. The dead-time varies between 150 μs and 2.5 ms and is given for each protein.

b

Ub, ubiquitin; ctAcP, common type acyl-phosphatase; DHFR, E.coli dihydrofolate reductase; αTS, α subunit of tryptophan synthase; cyt c, horse heart cytochrome c; apoMb, apomyoglobin; SMN, single-chain monellin; HO, heme-oxygenase.

c

When not explicitly given, estimates of the errors for unfolded and continuous-flow burst phase Rg are approximately ±1 Å and those of the native state are approximately ±0.2 Å.