Computational design of four-helix bundle proteins that bind nonbiological cofactors.
Recent work is discussed concerning the computational design of four-helix bundle proteins that form complexes with nonbiological cofactors. Given that often there are no suitable natural proteins to provide starting points in the creation of such nonbiological systems, computational design is well suited for the design and study of new protein-cofactor complexes. Recent design efforts are presented in the context of prior work on the de novo design and engineering of porphyrin-binding four-helix bundle proteins and current developments in nonlinear optical materials. Such protein-nonbiological cofactor complexes stand to enable new applications in protein science and materials research.
Lehmann
Andreas
A
Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104, USA.
Saven
Jeffery G
JG
D001665:Binding Sites; D003198:Computer Simulation; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
D011506:Proteins; D006418:Heme