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Natural supramolecular protein assemblies

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TLDR
This review illustrates that a striking structural diversity of protein assemblies is present in nature, and describes structure-function relationship studies for selected classes of protein architectures, and highlights the techniques that enable the characterisation of supramolecular protein structures.
Abstract
Supramolecular protein assemblies are an emerging area within the chemical sciences, which combine the topological structures of the field of supramolecular chemistry and the state-of-the-art chemical biology approaches to unravel the formation and function of protein assemblies. Recent chemical and biological studies on natural multimeric protein structures, including fibers, rings, tubes, catenanes, knots, and cages, have shown that the quaternary structures of proteins are a prerequisite for their highly specific biological functions. In this review, we illustrate that a striking structural diversity of protein assemblies is present in nature. Furthermore, we describe structure–function relationship studies for selected classes of protein architectures, and we highlight the techniques that enable the characterisation of supramolecular protein structures.

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Self-Assembled Peptide- and Protein-Based Nanomaterials for Antitumor Photodynamic and Photothermal Therapy.

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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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Chemical reactivity under nanoconfinement

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Chemistry Can Make Strict and Fuzzy Controls for Bio-Systems: DNA Nanoarchitectonics and Cell-Macromolecular Nanoarchitectonics

TL;DR: In this review, two kinds of bio-related nanoarchitectonics are introduced, DNA nano architectonics and cell-macromolecular nanoArchitectonics, both of which are basically controlled by chemical strategies.
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Bioengineered protein-based nanocage for drug delivery.

TL;DR: This article reviews various existing types of protein-based nanocages that are used for therapeutic purposes, and outlines their drug-loading mechanisms and bioengineering strategies via genetic and chemical functionalization.
References
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Collagen Structure and Stability

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Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore

TL;DR: The structure proves the heptameric subunit stoichiometry of the α-hemolysin oligomer, shows that a glycine-rich and solvent-exposed region of a water-soluble protein can self-assemble to form a transmembrane pore of defined structure, and provides insight into the principles of membrane interaction and transport activity of β barrel pore-forming toxins.
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The amyloid state and its association with protein misfolding diseases

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Actin structure and function.

TL;DR: Structures of G-actin and F-actIn are reviewed and some of the interactions that control the polymerization and disassembly of actin are discussed, which make actin a critical player in many cellular functions, ranging from cell motility and the maintenance of cell shape and polarity to the regulation of transcription.
Journal ArticleDOI

Chaperone machines for protein folding, unfolding and disaggregation

TL;DR: The structural basis of their mechanism of action is being unravelled and typically involves massive displacements of 20–30 kDa domains over distances of 20-50 Å and rotations of up to 100°.
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