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Open AccessJournal ArticleDOI

A Universal Chemical Method for Rational Design of Protein-Based Nanoreactors*.

TLDR
In this paper, Micelle-assisted protein labeling (MAPLab) technology along with the N-terminal bioconjugation strategy is utilized for the synthesis of a well-defined monodisperse self-assembling semi-synthetic protease.
Abstract
Self-assembly of a monomeric protease to form a multi-subunit protein complex "proteasome" enables targeted protein degradation in living cells. Naturally occurring proteasomes serve as an inspiration and blueprint for the design of artificial protein-based nanoreactors. Here we disclose a general chemical strategy for the design of proteasome-like nanoreactors. Micelle-assisted protein labeling (MAPLab) technology along with the N-terminal bioconjugation strategy is utilized for the synthesis of a well-defined monodisperse self-assembling semi-synthetic protease. The designed protein is programmed to self-assemble into a proteasome-like nanostructure which preserves the functional properties of native protease.

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Posted ContentDOI

Rational Design of Self-assembling Artificial Proteins Utilizing a Micelle-Assisted Protein Labeling Technology (MAPLabTech): Testing the Scope

TL;DR: In this article, the synthesis of self-assembling artificial proteins (SAPs) using micelle-assisted protein labeling technology (MAPLabTech) has been described by developing a chemical method for site-specific labeling of a surfaceexposed cysteine residue of globular proteins.
Journal ArticleDOI

Rational Design of Self‐Assembling Artificial Proteins Utilizing a Micelle‐Assisted Protein Labeling Technology (MAPLabTech): Testing the Scope **

TL;DR: The synthesis of novel SAPs are described by developing a chemical method for site‐specific labeling of a surface‐exposed cysteine residue of globular proteins and their systematic self‐assembly and disassembly studies using size‐exclusion chromatography are disclosed.
References
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Journal ArticleDOI

The coming of age of de novo protein design

TL;DR: De novo protein design explores the full sequence space, guided by the physical principles that underlie protein folding, to design new functional proteins from the ground up to tackle current challenges in biomedicine and nanotechnology.
Journal ArticleDOI

A protein catalytic framework with an N-terminal nucleophile is capable of self-activation

TL;DR: The name Ntn (N-terminal nucleophile) hydrolases is suggested for this structural superfamily of enzymes which appear to be evolutionarily related but which have diverged beyond any recog-nizable sequence similarity.
Journal ArticleDOI

Accurate design of megadalton-scale two-component icosahedral protein complexes.

TL;DR: Inspired by natural materials, the computational design and experimental characterization of co-assembling, two-component, 120-subunit icosahedral protein nanostructures with molecular weights and dimensions comparable to those of small viral capsids are reported.
Journal ArticleDOI

Protein-based organelles in bacteria: carboxysomes and related microcompartments

TL;DR: The carboxysome, a prototypical bacterial microcompartment that is found in cyanobacteria and some chemoautotrophs, encapsulates ribulose-1,5-bisphosphate carboxylase/oxygenase and carbonic anhydrase, and thereby enhances carbon fixation by elevating the levels of CO2 in the vicinity of RuBisCO.
Journal ArticleDOI

Protein Assembly: Versatile Approaches to Construct Highly Ordered Nanostructures

TL;DR: This Review outlines recent advances in the field of protein assembly and summarizes several strategies, including biotechnological strategies, chemical strategies, and combinations of these approaches, for manipulating proteins to self-assemble into desired nanostructures.
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