Minimalist Design of Allosterically Regulated Protein Catalysts

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations

Abstract

Nature facilitates chemical transformations with exceptional selectivity and efficiency. Despite a tremendous progress in understanding and predicting protein function, the overall problem of designing a protein catalyst for a given chemical transformation is far from solved. Over the years, many design techniques with various degrees of complexity and rational input have been developed. Minimalist approach to protein design that focuses on the bare minimum requirements to achieve activity presents several important advantages. By focusing on basic physicochemical properties and strategic placing of only few highly active residues one can feasibly evaluate in silico a very large variety of possible catalysts. In more general terms minimalist approach looks for the mere possibility of catalysis, rather than trying to identify the most active catalyst possible. Even very basic designs that utilize a single residue introduced into nonenzymatic proteins or peptide bundles are surprisingly active. Because of the inherent simplicity of the minimalist approach computational tools greatly enhance its efficiency. No complex calculations need to be set up and even a beginner can master this technique in a very short time. Here, we present a step-by-step protocol for minimalist design of functional proteins using basic, easily available, and free computational tools.

Original languageEnglish (US)
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Pages191-202
Number of pages12
DOIs
StatePublished - 2016

Publication series

NameMethods in Enzymology
Volume580
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • Calmodulin
  • Catalysis
  • Docking
  • Enzyme design
  • Esterase
  • Rosetta

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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