Diffraction to study protein and peptide assemblies

被引:35
作者
Makin, O. Sumner
Sikorski, Pawel
Serpell, Louise C.
机构
[1] Univ Sussex, Sch Life Sci, Dept Biochem, Brighton BN1 9QG, E Sussex, England
[2] Norwegian Univ Sci & Technol, Dept Phys, NO-7491 Trondheim, Norway
基金
英国惠康基金; 英国生物技术与生命科学研究理事会;
关键词
D O I
10.1016/j.cbpa.2006.08.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:417 / 422
页数:6
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