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Analysing structural data to explore the function of an essential bacterial protein foldase
Author(s) -
Samuel F. Haysom
Publication year - 2021
Publication title -
the biochemist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.126
H-Index - 7
eISSN - 1740-1194
pISSN - 0954-982X
DOI - 10.1042/bio_2021_166
Subject(s) - foldase , function (biology) , protein folding , visualization , computational biology , mechanism (biology) , biology , computer science , microbiology and biotechnology , groel , artificial intelligence , genetics , physics , escherichia coli , gene , quantum mechanics
Structural biology, or the study of how protein structures dictate their function, is a fundamental part of life science research, allowing the mechanisms underpinning life to be unravelled at the molecular level. Due to the complexity of 3D data, researchers often use special visualization methods to extract useful information from protein structures. This article uses the most common of these visualisation methods to examine different structures of the β-barrel assembly machinery complex (BAM), an essential protein that folds other proteins into the outer-membranes of Gram-negative bacteria. By exploring how BAM’s 3D shape changes as it interacts with its substrates throughout the folding process, it is possible to reconstruct a potential mechanism for this molecular machine that can be used to drive further research.

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