A conformational fingerprint for amyloidogenic light chains

Paissoni C, Puri S, Broggini L, Sriramoju M, Maritan M, Russo R, Speranzini V, Ballabio F Nuvolone M, Merlini G, Palladini G, Hsu S, Ricagno S, Camilloni C, eLife 13 (2025) DOI

SASDVL4 – Immunoglobulin light chain H3

Immunoglobulin light chain H3

MW^experimental	45	kDa
MW^expected	45	kDa
V^Porod	56	nm³

log I(s) 7.30×10² 7.30×10¹ 7.30×10⁰ 7.30×10^-1

Immunoglobulin light chain H3 small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

Immunoglobulin light chain H3 Guinier plot

ln 7.30×10² R_g: 2.6 nm 0 (2.6 nm)^-2 s²

(sR_g)²I(s)/I(0)

Immunoglobulin light chain H3 Kratky plot

1.104 0 √3 sR_g

p(r)	R_g: 2.6 nm 0 D_max: 8.4 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

0.000
1.154

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Immunoglobulin light chain H3 MODELLER model

Synchrotron SAXS data from solutions of immunoglobulin light chain H3 in 20 mM TrisHCL, 150 mM NaCl, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.124423 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.40 mg/ml was measured at 20°C. 20 successive 0.050 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.

Immunoglobulin light chain H3 (H3)
Mol. type		Protein
Organism		Homo sapiens
Olig. state		Dimer
Mon. MW		22.7 kDa
Sequence		FASTA

PDB ID		5MTL