Natural supramolecular protein assemblies

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...

Full description

Saved in:
Bibliographic Details
Published in:Chemical Society reviews 2016-01, Vol.45 (1), p.24-39
Main Authors: Pieters, Bas J. G. E, van Eldijk, Mark B, Nolte, Roeland J. M, Mecinovi, Jasmin
Format: Article
Language:English
Subjects:
Animals
Assemblies
Biological
Biological Products - chemical synthesis
Biological Products - chemistry
Biology
Cages
Humans
Knots
Models, Molecular
Multiprotein Complexes - chemical synthesis
Multiprotein Complexes - chemistry
Proteins
State of the art
Tubes
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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. Structural and functional studies on a diverse set of natural supramolecular protein assemblies are systematically presented in this Tutorial Review.
ISSN:0306-0012
1460-4744
DOI:10.1039/c5cs00157a