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


MWI(0) 49 kDa
MWexpected 55 kDa
VPorod 170 nm3
log I(s) 3.11×102 3.11×101 3.11×100 3.11×10-1
TET12(1.10)SN-f5(222CC) small angle scattering data  s, nm-1
ln I(s)
TET12(1.10)SN-f5(222CC) Guinier plot ln 3.11×102 Rg: 3.4 nm 0 (3.4 nm)-2 s2
TET12(1.10)SN-f5(222CC) Kratky plot 1.104 0 3 sRg
TET12(1.10)SN-f5(222CC) pair distance distribution function Rg: 3.5 nm 0 Dmax: 10.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
TET12(1.10)SN-f5(222CC) MODELLER model

log I(s)
 s, nm-1
TET12(1.10)SN-f5(222CC) DAMFILT model
TET12(1.10)SN-f5(222CC) DAMMIF model

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 (10-0.5 mg/mL) stock solutions. No dilution effects were observed.

TET12(1.10)SN-f5(222CC) (TET12SN(222CC))
Mol. type   Protein
Organism   synthetic construct
Olig. state   Monomer
Mon. MW   55.4 kDa
Sequence   FASTA