Journal article
DynaMut: Predicting the impact of mutations on protein conformation, flexibility and stability
CHM Rodrigues, DEV Pires, DB Ascher
Nucleic Acids Research | OXFORD UNIV PRESS | Published : 2018
DOI: 10.1093/nar/gky300
Open access
Abstract
Proteins are highly dynamic molecules, whose function is intrinsically linked to their molecular motions. Despite the pivotal role of protein dynamics, their computational simulation cost has led to most structure-based approaches for assessing the impact of mutations on protein structure and function relying upon static structures. Here we present DynaMut, a web server implementing two distinct, well established normal mode approaches, which can be used to analyze and visualize protein dynamics by sampling conformations and assess the impact of mutations on protein dynamics and stability resulting from vibrational entropy changes. DynaMut integrates our graph-based signatures along with nor..
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Awarded by Conselho Nacional de Desenvolvimento Científico e Tecnológico
Funding Acknowledgements
Australian Government Research Training Program Scholarship [to C.H.M.R]; Jack Brockhoff Foundation [JBF 4186, 2016 to D.B.A.]; Newton Fund RCUK-CONFAP Grant awarded by the Medical Research Council (MRC) and Fundacao de Amparoa Pesquisa do Estado de Minas Gerais (FAPEMIG) [MR/M026302/1 to D.B.A., D.E.V.P.]; National Health and Medical Research Council of Australia [APP1072476 to D.B.A.]; Victorian Life Sciences Computation Initiative (VLSCI), an initiative of the Victorian Government, Australia, on its Facility hosted at the University of Melbourne [UOM0017]; Instituto Rene Rachou (IRR/FIOCRUZ Minas), Brazil and Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) [to D.E.V.P.]; Department of Biochemistry and Molecular Biology, University of Melbourne [to D.B.A.]. Funding for open access charge: MRC.