Theoretical esterases: Difference between revisions
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== Background == | == Background == | ||
''De Novo'' protein design and synthesis has been a goal of biochemistry for decades and has wide sweeping implications in many fields. The advent of computers has given rise to computer programs such as RosettaMatch which are capable of identifying sequences compatible with given protein skeletons. In August of 2012, the Richter Lab and collaborators published an attempted to design an esterase from a theoretically functional protein backbone. This article is a summary of their contribution to the field of ''de Novo'' esterase design. | ''De Novo'' protein design and synthesis has been a goal of biochemistry for decades and has wide sweeping implications in many fields. The advent of computers has given rise to computer programs such as RosettaMatch which are capable of identifying sequences compatible with given protein skeletons. In August of 2012, the Richter Lab and collaborators published an attempted to design an esterase from a theoretically functional protein backbone. This article is a summary of their contribution to the field of ''de Novo'' esterase design. | ||
As described in Richter et al, esterases use serines and cysteines as nucleophilic donors in the first step of ester hydrolysis. Either the oxygen in the backbone or residues such as asparagine or glutamine deprotonate the nucleophile. Hydrogen bond donors such as the NH backbone or residues in the active site create an “oxyanion hole” to stabilize any oxyanion formed during catalysis. | |||
== Relevance == | == Relevance == | ||
