title: Controlling complexity and water penetration in functional de novo protein design.
abstract: Natural proteins are complex, and the engineering elements that support function and catalysis are obscure. Simplified synthetic protein scaffolds offer a means to avoid such complexity, learn the underlying principles behind the assembly of function and render the modular assembly of enzymatic function a tangible reality. A key feature of such protein design is the control and exclusion of water access to the protein core to provide the low-dielectric environment that enables enzymatic function. Recent successes in de novo protein design have illustrated how such control can be incorporated into the design process and have paved the way for the synthesis of nascent enzymatic activity in these systems.
authors.affiliation: Department of Biochemistry and Biophysics, The Johnson Research Foundation, University of Pennsylvania, Philadelphia, PA 19104, USA.
authors.forename: J L Ross
authors.initials: JL
authors.lastname: Anderson
authors.forename: Ronald L
authors.initials: RL
authors.lastname: Koder
authors.forename: Christopher C
authors.initials: CC
authors.lastname: Moser
authors.forename: P Leslie
authors.initials: PL
authors.lastname: Dutton
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D002384:Catalysis; D009682:Magnetic Resonance Spectroscopy; D008567:Membranes, Artificial; D011506:Proteins / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D008567:Membranes, Artificial; D011506:Proteins; D014867:Water