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. 2020 Oct 1;21(19):7280. doi: 10.3390/ijms21197280

Table 1.

Physicochemical properties of TFPs and experimental conditions for NMR measurements.

Protein pI Charges (+/−/His) a HI b Labeling Conc., mM pH T, °C Freq., MHz c PDB Ref
SLURP-1 5.2 8/10/1 0.04 13C, 15N 0.3 4.7 37 800 6ZZE 6ZZF This work
Lypd6 5.3 11/15/3 −0.58 13C, 15N/15N d 0.1 7.0 30/37 d 600/800 6IB6 This work
Lypd6b 6.7 10/11/8 −0.68 13C, 15N 0.2 5.5 30/37 d 600/800 6ZSO This work
Lynx2 4.5 5/8/0 0.07 13C, 15N 0.25/0.07 d 6.7 45/37 d 600/800 6ZSS This work
Lynx1 8.1 8/6/2 −0.32 15N 0.5 5.3 25 800 2L03 [11]
SLURP-2 6.5 5/6/5 0.10 13C, 15N 0.5 e/0.08 d 4.8 37 600 2N99 [32]
WTX-P33A 8.9 13/7/1 −0.39 15N 0.5 3.0 30 700 2MJ0 [43]
NTII 8.7 10/6/2 −1.10 15N 1.0 5.0 30 800 2MJ4 [44]

a The number of positively (“+”, Arg/Lys/N-terminus) and negatively (“−“, Asp/Glu/C-terminus) charged groups in the protein at neutral pH. The number of His residues, which could change their ionization state at a pH of about 6.0, is also shown. b Mean Kyte-Doolittle hydrophobicity index [45]. The maximum and minimum values of this index are +4.5 and −4.5 for poly-Ile and poly-Arg sequences, respectively. c 1H frequency of the NMR spectrometer, where the 15N relaxation was measured. d First value shows the sample, its concentration, or temperature used for structure calculation; the second shows the same value for the 15N relaxation measurements. e 5% dioxane was added to the sample to prevent aggregation.