Table 2. Representative Examples of Protein Resonance Assignment Using 1H Detection.
protein | size | labeling | strategies | time (days) | B0 (T) | νR (kHz) | extent | ref |
---|---|---|---|---|---|---|---|---|
microcrystalline | ||||||||
TS | 665 | 1HN, 2H, 13C, 15N | 4D C′αβNH,a 4D S2B,b 5D HNcCNH bwd/fwdc | 90 | 16.4 | 55 | bb (74.8%) | (204) |
MBP | 371 | 13C, 15N | RAVASSAd, HCCH-TOCSY | 14 | 18.8, 23.5 | 107 | bb (90%), sc (partial) | (151), 57 |
hCAII | 260 | 1HN, 2H, 13C, 15N | HNNH,e S2B,b C′αβNHa | 27.2 | 18.8 | 55 | bb (90%) | (203) |
ϵ186 | 179 | 13C, 15N | C′αβNHa | 7.1 | 18.8 | 60 | bb (74%) | (120) |
SOD | 153 | 1HN, 2H, 13C, 15N | C′αNHf | 5.6 | 23.5 | 60 | bb (95%) | (112) |
β2m | 99 | 1HN, 2H, 13C, 15N | C′αβNHa | 3.0 | 23.5 | 60 | bb (76%) | (198) |
membrane-embedded | ||||||||
CorA | 5 × 351 | 13C, 15N | C′αβNH,a Hα det. | 28.3 | 18.8, 23.5 | 107 | bb (35%, 54% in TM) | (224) |
hVDAC1 | 283 | 1HN, 2H, 13C, 15N | 3D/4D C′αβNH,a NNHe | 74.1 | 18.8, 22.3 | 55, 91 | bb (69%) | (225), 226 |
OmpG | 281 | 1HN 70/100%, 2H, 13C, 15N | C′αβNHa | 13.1 | 23.5 | 60 | bb (60%), sc (51%) | (198), (227) |
13C-selective | 13C det. | 21.4 | 13 | |||||
PR | 6 × 243 | 13C, 15N | C′αNH,f Hα-det., hCCH-TOCSY | 13.5 | 23.5 | 100 | bb (61%), sc (57%) | (228) |
AlkL | 203 | 13C, 15N | C′αβNH,a Hα-det., HCCH-TOCSY | 31.7 | 23.5 | 111 | bb (84%), sc (partial) | (60), (229) |
1HN, 2H, 13C, 15N | 22.1 | 18.8 | 60 | |||||
GlpG | 189 | 1HN, 2H, 13C, 15N | C′αβNHa | N/A | 14.1 | 40 | bb (60%) | (230) |
KCsA | 166 | iFD, 13C, 15N | C′αβNH,a13C-det. | 20.4 | 18.8 | 60 | bb (21% of TM) | (101), (231) |
M2 | 2 × 43 | 1HN, 2H, 13C, 15N | C′αβNHa | 13.7 | 23.5 | 60 | bb (51%) | (198) |
aggregates/assemblies/precipitates | ||||||||
FcRnECD | 373 | 13C, 15N | C′αNH,f CαCβNHg | N/A | 20 | 100 | bb (25 aa) | (232) |
TET-2 | 12 × 353 | 1HN, 2H, 13C, 15N | C′αβNHa | 11.1 | 14.1 | 38, 53 | bb (85%), sc (70%) | (223) |
13C, 15N | 13C-det. | 42.4 | 14.1, 23.5 | 15, 18 | ||||
aa. sel. 13C,15N | 13C-det. | 16.7 | 14.1 | 15 | ||||
ILV-CH3 | solution HMQC (mutagenesis) | ILV-CH3 (94) | ||||||
Cp149 | 149 | 13C, 15N | C′αβNHa | 15.5 | 20.0 | 100 | bb (85%) | (113) |
AP205CP | 180 × 130 | 13C, 15N | Hα-det., HCCH-TOCSY | 6.9 | 23.5 | 100 | bb (78%), sc (74%) | (111), (62) |
1HN, 2H, 13C, 15N | C′αβNHa | 6.7 | 23.5 | 60 | bb (72%) | (198) | ||
SSB | 110 | 13C, 15N | C′αβNHa | 7.1 | 18.8 | 60 | bb (75%) | (120) |
amyloid fibrils | ||||||||
BacA | 103 | 1HN, 2H, 13C, 15N | 3D C′αNHf | 8.0 | 21.2 | 40 | bb (93%) | (233) |
β2m | 99 | 1HN, 2H, 13C, 15N | 5D hNCCNH bwd/fwdh | 4.8 | 23.5 | 55 | bb (77%) | (234), (68) |
Tau | 96 | 13C, 15N | 4D C′αNH,f 3D CβNH, NNHe | 18.8 | 55 | bb (27%) | (199) | |
HELL-F | 51 | 13C, 15N | C′αβNH,a Hα-det., hCCH-TOCSY | 13.5 | 23.5 | 100 | bb (92%), sc (91%) | (215) |
Aβ1–42 | 42 | 13C, 15N | C′αβNHa | 3.5 | 23.5 | 100 | bb (100%), sc (100%) in 15–42 region | (61) |
Aβ1–42 | 42 | 13C, 15N | 3D/4D C′αβNHa | 6.3 | 18.8 | 90 | bb (76%), sc (∼54%) | (126) |
Val-rev. lab.13C, 15N | 17.6 | 80 |
C′αβNH = Cαi/i–1-Ni-Hi, C′i/i-1-Ni-Hi, Cβi/i–1-Ni-Hi.
S2B = side-chain to backbone correlations (CXi-Ni-Hi).
5D HNcCNH bwd/fwd = Hi–1-Ni–1-C′i–1-Ni-Hi + Hi+1-Ni+1-Cαi-Ni-Hi.
Simultaneous Ni–1-Ni-Hi, Cαi+1-Cαi- Hαi, Cαi/i–1-Ni-Hi, Ni/i+1-Cαi-Hαi correlations + Cβi-Cαi-Hαi + Cβi-Ni-Hi.
HNNH and NNH = (Hi±1-) Ni±1-Ni-Hi.
C′αNH = Cαi/i–1-Ni-Hi, C′i/i-1-Ni-Hi.
CαCβNH = Cβi/i–1Cαi/i–1-Ni-Hi.
5D hNCCNH bwd/fwd = APSY Ni–1-Cαi–1-C′i–1-Ni-Hi + Ni+1-C′i-Cαi-Ni-Hi.