Clinically Linked Mutations in the Central Domains of Cardiac Myosin-Binding Protein C with Distinct Phenotypes Show Differential Structural Effects.

Nadvi NA, Michie KA, Kwan AH, Guss JM, Trewhella J, Structure 24(1):105-115 (2016) Europe PMC

SASDB25 – Cardiac myosin binding protein-C: domains C5-C6-C7

Cardiac myosin binding protein-C: domains C5-C6-C7
MWexperimental 38 kDa
MWexpected 36 kDa
VPorod 55 nm3
log I(s) 1.05×10-1 1.05×10-2 1.05×10-3 1.05×10-4
Cardiac myosin binding protein-C: domains C5-C6-C7 small angle scattering data  s, nm-1
ln I(s)
Cardiac myosin binding protein-C: domains C5-C6-C7 Guinier plot ln 1.06×10-1 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
Cardiac myosin binding protein-C: domains C5-C6-C7 Kratky plot 1.104 0 √3 sRg
p(r)
Cardiac myosin binding protein-C: domains C5-C6-C7 pair distance distribution function Rg: 3.9 nm 0 Dmax: 14.1 nm

Data validation

There are no models related to this curve.

X-ray synchrotron radiation scattering data from solutions of human cardiac myosin binding protein-C, domains C5-C6-C7 in 25 mM TrisHCl 250 mM NaCl, 2 mM TCEP, 0.02% sodium azide were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M-W pixel detector (I(s) vs s; s = 4π sin θ/λ, where 2θ is the scattering angle and λ=0.10332 nm). Different solute concentrations in the range 0.70-3.40 mg/ml were measured using a total exposure time of 44 s (recorded as 44 x 1 s frames). The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering from the matched solvent-blank was subtracted. The data presented here represent the SAXS profile extrapolated to zero concentration calculated from the solute concentration series.

Wavelength = UNKNOWN

Cardiac myosin binding protein-C: domains C5-C6-C7 (cMyBP-C)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   35.8 kDa
 
UniProt   Q14896 (641-964)
Sequence   FASTA