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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

SAXSMoW 2.0: Online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale

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Author(s):
Piiadov, Vassili [1] ; de Araujo, Evandro Ares [1] ; Oliveira Neto, Mario [2] ; Craievich, Aldo Felix [3] ; Polikarpov, Igor [1]
Total Authors: 5
Affiliation:
[1] Univ Sao Paulo, Inst Phys Sao Carlos, Sao Carlos, SP - Brazil
[2] Univ Estadual Paulista, Inst Biosci, Botucatu, SP - Brazil
[3] Univ Sao Paulo, Inst Phys, Sao Paulo, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Protein Science; v. 28, n. 2, p. 454-463, FEB 2019.
Web of Science Citations: 8
Abstract

Knowledge of molecular weight, oligomeric states, and quaternary arrangements of proteins in solution is fundamental for understanding their molecular functions and activities. We describe here a program SAXSMoW 2.0 for robust and quick determination of molecular weight and oligomeric state of proteins in dilute solution, starting from a single experimental small-angle scattering intensity curve, I(q), measured on a relative scale. The first version of this calculator has been widely used during the last decade and applied to analyze experimental SAXS data of many proteins and protein complexes. SAXSMoW 2.0 exhibits new features which allow for the direct input of experimental intensity curves and also automatic modes for quick determinations of the radius of gyration, volume, and molecular weight. The new program was extensively tested by applying it to many experimental SAXS curves downloaded from the open databases, corresponding to proteins with different shapes and molecular weights ranging from similar to 10 kDa up to about similar to 500 kDa and different shapes from globular to elongated. These tests reveal that the use of SAXSMoW 2.0 allows for determinations of molecular weights of proteins in dilute solution with a median discrepancy of about 12% for globular proteins. In case of elongated molecules, discrepancy value can be significantly higher. Our tests show discrepancies of approximately 21% for the proteins with molecular shape aspect ratios up to 18. (AU)

FAPESP's process: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation
Grantee:Igor Polikarpov
Support type: Research Projects - Thematic Grants
FAPESP's process: 14/00769-5 - Structural studies of glycoside hydrolyses in solution using small-angle scattering (SAS) techniques
Grantee:Vasilii Piiadov
Support type: Scholarships in Brazil - Doctorate (Direct)