BRANEart is a fast and accurate method to evaluate the contribution of each residue to the overall stability of membrane proteins and to identify interesting residues to mutate in view of modulating stability.

It is based on an extended set of membrane statistical potentials, which we have recently introduced [2]. These potentials are derived from a dataset of experimental membrane proteins with experimentally solved three-dimensional structure, and better describe the stability properties of this class of proteins than potentials derived from globular proteins. A combination of these potentials has been set up to identify residues that contribute favorably or unfavorably to the folding free energy in the transmembrane, inner or outer regions of the protein. Following an approach that is similar to the one used by SWOTein [3] for globular proteins, the residues are colored using a green to blue scale. Residues that contribute favorably in the lipidic environment of the transmembrane regions are defined as stability strengths and are colored in green, whereas residues that have an unfavorable contribution are identified as stability weaknesses and are colored in blue. For the aqueous environment outside the membrane, the conventions are opposite: stability strengths are colored in blue and weaknesses in green.

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[1] S. Basu, S. Assaff, F. Teheux, M. Rooman, F. Pucci (2021), BRANEart: identify stability strength and weakness regions in membrane proteins, Frontiers in Bioinformatics 1, 742843.

[2] M. N. Mbaye, Q. Hou, S. Basu, F. Teheux, F. Pucci, M. Rooman (2019), A comprehensive computational study of amino acid interactions in membrane proteins, Scientific Report 9, 12043.

[3] Q. Hou, F. Pucci, F. Ancien, J.M. Kwasigroch, R. Bourgeas, M. Rooman (2020), SWOTein: A structure-based approach to predict stability Strengths and Weaknesses of prOTEINs, Bioinformatics, btab034