Journal article

ThermoMutDB: a thermodynamic database for missense mutations.

Joicymara S Xavier, Thanh-Binh Nguyen, Malancha Karmarkar, Stephanie Portelli, Pâmela M Rezende, João PL Velloso, David B Ascher, Douglas EV Pires

Nucleic Acids Research | Oxford University Press | Published : 2020

Abstract

Proteins are intricate, dynamic structures, and small changes in their amino acid sequences can lead to large effects on their folding, stability and dynamics. To facilitate the further development and evaluation of methods to predict these changes, we have developed ThermoMutDB, a manually curated database containing >14,669 experimental data of thermodynamic parameters for wild type and mutant proteins. This represents an increase of 83% in unique mutations over previous databases and includes thermodynamic information on 204 new proteins. During manual curation we have also corrected annotation errors in previously curated entries. Associated with each entry, we have included information ..

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Grants

Awarded by Fundacao de Amparo a Pesquisa do Estado de Minas Gerais (FAPEMIG)


Awarded by Jack Brockhoff Foundation


Awarded by Wellcome Trust


Awarded by National Health and Medical Research Council (NHMRC) of Australia


Funding Acknowledgements

D.B.A. and D.E.V.P. were funded by a Newton Fund RCUK-CONFAP Grant awarded by the Medical Research Council (MRC) and Fundacao de Amparo a Pesquisa do Estado de Minas Gerais (FAPEMIG) [MR/M026302/1]; Conselho Nacional de Desenvolvimento Cientifico e Tecnol ' ogico (CNPq); Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES); Jack Brockhoff Foundation [JBF 4186, 2016]; Wellcome Trust [200814/Z/16/Z]; Investigator Grant from the National Health and Medical Research Council (NHMRC) of Australia [GNT1174405]. Funding for open access charge: Wellcome Trust.