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. 2022 May 10;122(10):9943–10018. doi: 10.1021/acs.chemrev.1c00918

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)
1–42 42 13C, 15N C′αβNHa 3.5 23.5 100 bb (100%), sc (100%) in 15–42 region (61)
1–42 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    
a

C′αβNH = Cαi/i–1-Ni-Hi, C′i/i-1-Ni-Hi, Cβi/i–1-Ni-Hi.

b

S2B = side-chain to backbone correlations (CXi-Ni-Hi).

c

5D HNcCNH bwd/fwd = Hi–1-Ni–1-C′i–1-Ni-Hi + Hi+1-Ni+1-Cαi-Ni-Hi.

d

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.

e

HNNH and NNH = (Hi±1-) Ni±1-Ni-Hi.

f

C′αNH = Cαi/i–1-Ni-Hi, C′i/i-1-Ni-Hi.

g

CαCβNH = Cβi/i–1i/i–1-Ni-Hi.

h

5D hNCCNH bwd/fwd = APSY Ni–1-Cαi–1-C′i–1-Ni-Hi + Ni+1-C′i-Cαi-Ni-Hi.