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

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.contributorBrazilian Center for Research in Energy and Materials-
Autor(es): dc.creatorde Oliveira Neto, Mario-
Autor(es): dc.creatorde Freitas Fernandes, Adriano-
Autor(es): dc.creatorPiiadov, Vassili-
Autor(es): dc.creatorCraievich, Aldo Felix-
Autor(es): dc.creatorde Araújo, Evandro Ares-
Autor(es): dc.creatorPolikarpov, Igor-
Data de aceite: dc.date.accessioned2025-08-21T15:49:32Z-
Data de disponibilização: dc.date.available2025-08-21T15:49:32Z-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2021-12-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1002/pro.4227-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/222891-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/222891-
Descrição: dc.descriptionSAXSMoW (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 weights. Our results demonstrate that most of the molecular weights determined for the nonglycosylated and also for the glycosylated proteins are in good agreement with their expected molecular weights. Additionally, the average discrepancies between the calculated molecular weights and their nominal values for glycosylated proteins are similar to those for nonglycosylated ones.-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionBiophysics and Pharmacology Department Bioscience Institute Universidade Estadual Paulista, São Paulo-
Descrição: dc.descriptionSao Carlos Institute of Physics University of Sao Paulo-
Descrição: dc.descriptionDepartment of Applied Physics University of Sao Paulo, São Paulo-
Descrição: dc.descriptionBrazilian Synchrotron Light Laboratory Brazilian Center for Research in Energy and Materials, São Paulo-
Descrição: dc.descriptionBiophysics and Pharmacology Department Bioscience Institute Universidade Estadual Paulista, São Paulo-
Descrição: dc.descriptionCNPq: 140739/2017-3-
Descrição: dc.descriptionFAPESP: 2015/13684-0-
Descrição: dc.descriptionFAPESP: 2018/22300-0-
Descrição: dc.descriptionCNPq: 303988/2016-9-
Descrição: dc.descriptionCNPq: 307490/2019-0-
Descrição: dc.descriptionCNPq: 310531/2019-5-
Formato: dc.format251-258-
Idioma: dc.languageen-
Relação: dc.relationProtein Science-
???dc.source???: dc.sourceScopus-
Título: dc.titleSAXSMoW 3.0: New advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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