Binding by calmodulin is coupled to transient unfolding of the third FF domain of Prp40A.

Díaz Casas A, Cordoba JJ, Ferrer BJ, Balakrishnan S, Wurm JE, Pastrana-Ríos B, Chazin WJ, Protein Sci 32(4):e4606 (2023) Europe PMC

SASDPV6 – Calmodulin

Calmodulin-1
MWexperimental 16 kDa
MWexpected 17 kDa
VPorod 38 nm3
log I(s) 6.16×101 6.16×100 6.16×10-1 6.16×10-2
Calmodulin-1 small angle scattering data  s, nm-1
ln I(s)
Calmodulin-1 Guinier plot ln 6.16×101 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
Calmodulin-1 Kratky plot 1.104 0 3 sRg
p(r)
Calmodulin-1 pair distance distribution function Rg: 2.2 nm 0 Dmax: 7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of calmodulin in 50 mM HEPES, 100 mM NaCl, 2 mM CaCl2, 1 mM TCEP, pH 7.4 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 8.00 mg/ml was measured at 25°C. 800 successive 3 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Calmodulin-1
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   16.8 kDa
 
UniProt   P0DP23 (1-149)
Sequence   FASTA