Understanding protein self-assembly is important for many biological and industrial processes. Proteins can self-assemble into crystals, filaments, gels, and other amorphous aggregates. The final forms include virus capsids and condensed phases associated with diseases such as amyloid fibrils. Although seemingly different, these assemblies all originate from fundamental protein interactions and are driven by similar thermodynamic and kinetic factors. Here we review recent advances in understanding protein self-assembly through a soft condensed matter perspective with an emphasis on three specific systems: globular proteins, viruses, and amyloid fibrils. We conclude with a discussion of unanswered questions in the field.

The physics of protein self-assembly

Emanuela Zaccarelli;
2016

Abstract

Understanding protein self-assembly is important for many biological and industrial processes. Proteins can self-assemble into crystals, filaments, gels, and other amorphous aggregates. The final forms include virus capsids and condensed phases associated with diseases such as amyloid fibrils. Although seemingly different, these assemblies all originate from fundamental protein interactions and are driven by similar thermodynamic and kinetic factors. Here we review recent advances in understanding protein self-assembly through a soft condensed matter perspective with an emphasis on three specific systems: globular proteins, viruses, and amyloid fibrils. We conclude with a discussion of unanswered questions in the field.
2016
Istituto dei Sistemi Complessi - ISC
Inglese
22
April
73
79
7
https://www.sciencedirect.com/science/article/pii/S1359029416300292
Sì, ma tipo non specificato
Amyloids
Crystallization
Patchy colloids
Protein
Self-assembly
Soft matter
Virus capsids
Available online 25 March 2016.
4
info:eu-repo/semantics/article
262
Mcmanus, Jennifer J.; Charbonneau, Patrick; Zaccarelli, Emanuela; Asherie, Neer
01 Contributo su Rivista::01.01 Articolo in rivista
open
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/316098
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