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Nat Struct Mol Biol. 2016 Jun 7;23(6):475-80. doi: 10.1038/nsmb.3231.

Toward high-resolution computational design of the structure and function of helical membrane proteins.

Author information

1
Structural and Computational Biology and Molecular Biophysics Graduate Program, Baylor College of Medicine, Houston, Texas, USA.
2
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, USA.
3
Department of Pharmacology, Baylor College of Medicine, Houston, Texas, USA.
4
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.

Abstract

The computational design of α-helical membrane proteins is still in its infancy but has already made great progress. De novo design allows stable, specific and active minimal oligomeric systems to be obtained. Computational reengineering can improve the stability and function of naturally occurring membrane proteins. Currently, the major hurdle for the field is the experimental characterization of the designs. The emergence of new structural methods for membrane proteins will accelerate progress.

PMID:
27273630
PMCID:
PMC4962061
DOI:
10.1038/nsmb.3231
[Indexed for MEDLINE]
Free PMC Article

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