Applications of sequence coevolution in membrane protein biochemistry.

Autor: Nicoludis JM; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, United States., Gaudet R; Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA, 02138, United States. Electronic address: gaudet@mcb.harvard.edu.
Jazyk: angličtina
Zdroj: Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2018 Apr; Vol. 1860 (4), pp. 895-908. Date of Electronic Publication: 2017 Oct 07.
DOI: 10.1016/j.bbamem.2017.10.004
Abstrakt: Recently, protein sequence coevolution analysis has matured into a predictive powerhouse for protein structure and function. Direct methods, which use global statistical models of sequence coevolution, have enabled the prediction of membrane and disordered protein structures, protein complex architectures, and the functional effects of mutations in proteins. The field of membrane protein biochemistry and structural biology has embraced these computational techniques, which provide functional and structural information in an otherwise experimentally-challenging field. Here we review recent applications of protein sequence coevolution analysis to membrane protein structure and function and highlight the promising directions and future obstacles in these fields. We provide insights and guidelines for membrane protein biochemists who wish to apply sequence coevolution analysis to a given experimental system.
(Copyright © 2017 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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