2013Unpublished venueRequires access

Rational Design of Protein Cages for Alternative Enzymatic Functions

Nicholas Marshall, Kyle D. Miner, Tiffany D. Wilson, Yi Lu

Open publisher page 6 citations

Abstract

This chapter discusses several studies from various classes of metalloenzymes, in which a functional property of the protein, such as electron transfer or catalysis, was either predictably improved or completely altered, or cases where new functionality was engineered into a protein scaffold by modifying the protein cage, as opposed to the catalytic site itself. The chapter focuses on inorganic chemistry, special emphasis is given to metalloenzymes and, where available, the methods used in each study in order to serve as a guide for future studies in metalloenzyme design and engineering. The recent progress in rational design of protein cages for alternative enzymatic functions, and in particular, studies that have strived to predictably alter or impart new functionality to metalloenzymes, have led to important advances in our knowledge of how metalloenzymes work and have set the groundwork for producing designer proteins with a selected function and high rates of catalysis.

About this research paper

What this paper is about

This chapter discusses several studies from various classes of metalloenzymes, in which a functional property of the protein, such as electron transfer or catalysis, was either predictably improved or completely altered, or cases where new functionality was engineered into a protein scaffold by modifying the protein cage, as opposed to the catalytic site itself. The chapter focuses on inorganic chemistry, special emphasis is given to metalloenzymes and, where available, the methods used in each study in order to serve as a guide for future studies in metalloenzyme design and engineering. The recent progress in rational design of protein cages for alternative enzymatic functions, and in particular, studies that have strived to predictably alter or impart new functionality to metalloenzymes, have led to important advances in our knowledge of how metalloenzymes work and have set the groundwork for producing designer proteins with a selected function and high rates of catalysis.

Why it matters

OpenAlex reports 6 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

This chapter discusses several studies from various classes of metalloenzymes, in which a functional property of the protein, such as electron transfer or catalysis, was either predictably improved or completely altered, or cases where new functionality was engineered into a protein scaffold by modifying the protein cage, as opposed to the catalytic site itself. The chapter focuses on inorganic chemistry, special emphasis is given to metalloenzymes and, where available, the methods used in each study in order to serve as a guide for future studies in metalloenzyme design and engineering. The recent progress in rational design of protein cages for alternative enzymatic functions, and in particular, studies that have strived to predictably alter or impart new functionality to metalloenzymes, have led to important advances in our knowledge of how metalloenzymes work and have set the groundwork for producing designer proteins with a selected function and high rates of catalysis.

Key concepts: Rational design, Protein design, Protein engineering, Biochemical engineering, Protein function, Function (biology), Chemistry, Design elements and principles

Related papers

Back to paper searchBrowse research topicsOriginal source
Rational Design of Protein Cages for Alternative Enzymatic Functions — Research Paper | ScholarLens