Correction to: A suite of 19 F based relaxation dispersion experiments to assess biomolecular motions
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CORRECTION
Correction to: A suite of 19F based relaxation dispersion experiments to assess biomolecular motions Jan H. Overbeck1 · Werner Kremer1 · Remco Sprangers1 Published online: 25 November 2020 © Springer Nature B.V. 2020
Correction to: Journal of Biomolecular NMR https://doi.org/10.1007/s10858-020-00348-4
The original article has been corrected.
In the original publication, Figures 3 and 6 were displayed incorrectly due to a mistake made by the publisher. The correct version of Figs. 3 and 6 are given below. anti-ringing φ5
19F
φ1 φ2 φ3
Tmax - TSL
TSL
80 1
0.5
0
40
0
0.02
ex
351 Hz
50
1
20
[s -1 ]
Intensity
60
7859 Hz
22
W7
0.04
R2 + R
R2 + R
ex
[s -1 ]
70
|ΔωW29|= 0.51 ± 0.02 ppm
heating compensation
spin lock
B
pA = 96.6 ± 0.4 % kex = 2286 ± 268 s-1 |ΔωW7|= 2.62 ± 0.18 ppm
time [s]
30 20
Intensity
A
φ4
18 16
7859 Hz
W29
0.5
351 Hz 0
0
0.02
0.04
time [s]
14 12 10
10 0
2000
4000
/2 SL
6000
8000
[s -1 ]
Fig. 3 19F on-resonance R 1ρ experiment. a Pulse sequence for the 19 F on-resonance R 1ρ experiment. Narrow (wide) rectangles indicate 90° (180°) pulses, which are applied along the x-axis unless indicated otherwise. The phase cycle is φ1 = x, φ2 = [− x, x], φ3 = [x, x, − x,
0
2000
4000
/2 SL
6000
8000
[s -1 ]
− x, y, y, − y, − y], φ4 = [y], φ5 = [− y], φrec = [x, − x, − x, x, y, − y, − y, y]. b On-resonance R1ρ relaxation dispersion profiles for W7 and W29. The size of the error-bars correspond to 1 standard deviation
The original article can be found online at https://doi.org/10.1007/ s10858-020-00348-4. * Remco Sprangers [email protected] 1
Department of Biophysics I, Regensburg Center for Biochemistry, University of Regensburg, 93053 Regensburg, Germany
13
Vol.:(0123456789)
768
Journal of Biomolecular NMR (2020) 74:767–768
A
B
293 K
265 260 255 250
293 K
255 250 245 240 235 230
303 K
190
180
303 K
190
R 2 + R ex [s -1 ]
F
10000
185 180 175 170
0.9 300
310
320
ΔH TΔS
330
R eff [s -1 ] 2
) eq
ln(k,K
-ln(Keq) 3.2
3.3
1/T [1/K]
GS
3.4 10
k1 k-1
-3
Fig. 6 19F Relaxation dispersion experiments of the 360 kDa α7α7 double heptamer. a Model of the double heptameric α7α7 complexes with 14 BTFA labeling sites at position 18C (purple) of each subunit. Position 35 that does not show exchange (Fig. S8) is indicated in cyan. The model of the complex is based on the structure of the 20S proteasome from T. acidophilum (PDB ID 1PMA). b CPMG experiPublisher’s Note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
13
100 95 90
ES
145 140 135 130 125 110
323 K
105
4
3.1
130
313 K
150
120
ln(k1)
6
135
125
ln(k-1)
8
2
140
T [K]
10
313 K
145
ΔG
R 2 + R ex [s -1 ]
290
ES
GS
R 2 + R ex [s -1 ]
kcal/mol
pA
0 1
E
170
TS
5000
R eff [s -1 ] 2
k ex [s -1 ]
R eff [s -1 ] 2
245 200
D
C R 2 + R ex [s -1 ]
R eff [s -1 ] 2
270
323 K
105 100 95 90 85
85 0
2000
4000
/2
CPMG
6000 -1
[s
8000
]
10000
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