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. Author manuscript; available in PMC: 2016 Mar 21.
Published in final edited form as: Biochemistry. 2015 Sep 11;54(38):5815–5827. doi: 10.1021/acs.biochem.5b00746

Table 2.

Best-Fit Solutions of Cyclophilin Microscopic Rate Constantsa

CypA CypB CypC GeoCyp
kAB (×106 s−1 M−1) 3.2 ± 0.2 2.1 ± 0.2 4.2 ± 0.8 5.2 ± 1.8
kBA (s−1) 550 ± 160 960 ± 430 1620 ± 820 720 ± 270
kBC (s−1) 1660 ± 660 550 ± 290 370 ± 170 2410 ± 1330
kCB (s−1) 1070 ± 230 320 ± 100 210 ± 50 810 ± 370
kCD (s−1) 170 ± 40 200 ± 70 260 ± 100 50 ± 10
kDC (×106 s−1 M−1) 10.0 ± 0.3 4.9 ± 0.2 7.9 ± 0.3 7.0 ± 0.1
KD-cis (µM) 17 ± 4 40 ± 14 32 ± 11 7 ± 1
KD-trans (µM) 170 ± 50 460 ± 230 400 ± 180 140 ± 30
bound cis/trans 1.6 ± 0.8 2.1 ± 1.5 2.1 ± 1.4 3.1 ± 1.0
ωtrans-bound D6 (ppm) 8.65 ± 0.04 8.63 ± 0.07 8.63 ± 0.06 8.14 ± 0.50
ωcis-bound D6 (ppm) 8.43 ± 0.03 9.76 ± 0.96 8.20 ± 1.05 8.93 ± 0.04
ωtrans-bound L7 (ppm) 8.30 ± 0.01 8.38 ± 0.05 8.36 ± 0.04 8.05 ± 0.16
ωcis-bound L7 (ppm) 8.26 ± 0.01 8.25 ± 0.02 8.23 ± 0.05 8.36 ± 0.07
a

Standard deviation determined from the 20 best fits to the data.