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
| Autor: | Aldo F. Craievich, Mario de Oliveira Neto, Evandro Ares de Araújo, Adriano de Freitas Fernandes, Vassili Piiadov, Igor Polikarpov |
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| Přispěvatelé: | Universidade Estadual Paulista (UNESP), Universidade de São Paulo (USP), Brazilian Center for Research in Energy and Materials |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Relative scale
Molecular mass Tools for Protein Science Chemistry Small-angle X-ray scattering Scattering Analytical chemistry Proteins computer.file_format Molecular Dynamics Simulation PROTEÍNAS Protein Data Bank Biochemistry Molecular Weight Protein structure X-Ray Diffraction Scattering Small Angle Databases Protein Molecular Biology computer Intensity (heat transfer) Software |
| Zdroj: | Protein Sci Scopus Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| Popis: | Made available in DSpace on 2022-04-28T19:47:17Z (GMT). No. of bitstreams: 0 Previous issue date: 2022-01-01 Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) 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 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. Biophysics and Pharmacology Department Bioscience Institute Universidade Estadual Paulista, São Paulo Sao Carlos Institute of Physics University of Sao Paulo Department of Applied Physics University of Sao Paulo, São Paulo Brazilian Synchrotron Light Laboratory Brazilian Center for Research in Energy and Materials, São Paulo Biophysics and Pharmacology Department Bioscience Institute Universidade Estadual Paulista, São Paulo CNPq: 140739/2017-3 FAPESP: 2015/13684-0 FAPESP: 2018/22300-0 CNPq: 303988/2016-9 CNPq: 307490/2019-0 CNPq: 310531/2019-5 |
| Databáze: | OpenAIRE |
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