SAXSMoW 3.0: New advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale

Abstract

SAXSMoW (SAXS Molecular Weight) is an online platform widely used over the past few years for determination of molecular weights of proteins in dilute solutions. The scattering intensity retrieved from small-angle X-ray scattering (SAXS) raw data is the sole input to SAXSMoW for determination of molecular weights of proteins in liquid. The current updated SAXSMoW version 3.0 determines the linear dependence of the true protein volume on their apparent protein volume, based on SAXS curves calculated for 67,000 protein structures selected from the Protein Data Bank. SAXSMoW 3.0 was tested against 43 experimental SAXS scattering curves from proteins with known molecular

In Vivo Incorporation of Photoproteins into GroEL Chaperonin Retaining Major Structural and Functional Properties

“…It is interesting that after correction on the protein concentration, the I(0) values for both populations are close to each other, hinting at the proximity of the molecular weights of these proteins. The other possibility to estimate independently the Guinier parameters and molecular weight of the proteins studied is represented in the recent works of Piiadov et al [ 31 , 32 ]. We uploaded our SAXS data to the online calculator described in these works and obtained the following results.…”

“…The Rg decrease may be caused by both the EGFP incorporation into the GroEL 14 inner cavity because it reflects an increase in the protein density arising with proximity to the protein center of mass and the decrease in the protein hydrodynamic size. Unfortunately, the molecular weight of the protein studied is closely related to the radius of gyration in the approach proposed by Piiadov et al [ 31 , 32 ], and the reason for the Rg value change is not taken into account. Nevertheless, within the error of the method [ 31 ], the molecular weight estimated seems to be real for GroEL 14 .…”

Human gingival mesenchymal stem cells-lyosecretome attenuates adverse effect of hydrogen peroxide-induced oxidative stress on osteoblast cells

“… 24 In this study, proteins in secretome and lyosecretome obtained from hGMSCs are thought to have protein types such as α-2-macroglobulin, Fa1p, peptide binding proteins 72/74, α-(1,4)-glucosidase, heat shock cognate 71 kDa protein, extracellular matrix protein-1, α-tubulin, and chymotrypsinogen. 31 , 32 , 33 , 34 , 35 , 36 , 37 For instance, α-2-macroglobulin functions as an extracellular macromolecule with a broad-spectrum protease inhibitory role. It serves as an ideal substrate for various catalytic types of endopeptidases.…”

Characterization of Surfactant Spheroidal Micelle Structure for Pharmaceutical Applications: A Novel Analytical Framework

“…In the following: (i) we discuss how to graphically estimate-from the PDF first derivative-the core and shell sizes of the micelle under study; (ii) we derive analytical equations useful both for determining the core-shell and shell-buffer electron density contrasts, starting from the core and shell sizes derived graphically; (iii) we apply the new proposed graphical-analytical approach, whose mathematical details are reported in Appendix A, to micelles formed by different surfactants that have been previously characterized, namely PS20 [12], DPC and SDS [13], and VitE-TPGS with and without a PSC [4]. This comparison with literature data helped us validate the new graphicalanalytical method and demonstrate its potentiality compared to the conventional approach based on the current SAXS/PDF simulation software [5][6][7][8][9][10].…”

“…SAXSMoW [9,10], an online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data.…”