Toward high-resolution computational design of the structure and function of helical membrane proteins.
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.
Structural and Computational Biology and Molecular Biophysics Graduate Program, Baylor College of Medicine, Houston, Texas, USA.|Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, USA.|Department of Pharmacology, Baylor College of Medicine, Houston, Texas, USA.
Patrick
P
Barth
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, USA.
Alessandro
A
Senes
D000252:Calcium-Transporting ATPases / Q000737:chemistry*; D017076:Computer-Aided Design; D004926:Escherichia coli / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D009004:Monosaccharide Transport Proteins / Q000737:chemistry*; D015202:Protein Engineering; D055550:Protein Stability; D017433:Protein Structure, Secondary; D012107:Research Design; D027981:Symporters / Q000737:chemistry*; D013816:Thermodynamics
D029968:Escherichia coli Proteins; C050221:LacY protein, E coli; D009004:Monosaccharide Transport Proteins; D027981:Symporters; D000252:Calcium-Transporting ATPases