Diffraction to study protein and peptide assemblies

Makin, O Sumner, Sikorski, Pawel and Serpell, Louise C (2006) Diffraction to study protein and peptide assemblies. Current Opinion in Chemical Biology, 10 (5). pp. 417-422. ISSN 1367-5931

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Abstract

Proteins and peptides are able to self-assemble in vivo and in vitro. In vitro, this ability can be exploited to make bionanomaterials with many potential uses. Peptides are capable of forming a wide range of structures including fibres, tubules and scaffolds. In vivo, proteins assemble to form cellular fibrous proteins, as well as being involved in protein misfolding in disease. Recent advances using X-ray diffraction have highlighted the internal structure of self-assembled proteins and peptides, showing packing of side chain residues and have enabled a deeper understanding of mechanisms of assembly.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Osmar Sumner Makin
Date Deposited: 06 Feb 2012 20:29
Last Modified: 22 Mar 2012 12:19
URI: http://sro.sussex.ac.uk/id/eprint/26092
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