Designed folding pathway of modular coiled-coil-based proteins.

Aupič J, Strmšek Ž, Lapenta F, Pahovnik D, Pisanski T, Drobnak I, Ljubetič A, Jerala R, Nat Commun 12(1):940 (2021) Europe PMC

SASDKQ2 – TET12SN(2CC)

TET12(1.10)SN-f5(2CC)

MW^I(0)	51	kDa
MW^expected	55	kDa
V^Porod	158	nm³

log I(s) 3.42×10^-2 3.42×10^-3 3.42×10^-4 3.42×10^-5

TET12(1.10)SN-f5(2CC) small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 3.43×10^-2 R_g: 3.4 nm 0 (3.4 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 3.4 nm 0 D_max: 9.6 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.3

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.093
1.070

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

SAXS experiments were carried out at P12 beamline at PETRA-III synchrotron (DESY, Hamburg, Germany). X-ray wavelength was 1.24 Å, the Pilatus 6M detector was positioned 3 m from the sample and the scattering vector ranged from 0.028-7.3 nm-1. Samples (30-40 µL) were measured using robotic sample handler in flow-through mode, to avoid radiation damage. For each sample, data was collected over 40 frames lasting 0.1 s. Frames not displaying any radiation damage were then automatically averaged. Before and after each sample, buffer scattering was collected and subtracted from sample scattering. To assess concentration effects, a dilution series consisting of 4 concentrations was measured. The dilution series were prepared from high concentration (8-0 mg/mL) stock solutions. No dilution effects were observed.

TET12(1.10)SN-f5(2CC) (TET12SN(2CC))
Mol. type		Protein
Organism		synthetic construct
Olig. state		Monomer
Mon. MW		54.8 kDa
Sequence		FASTA