@article { ISI:000322752900022,
	title = {Highly Ordered Protein Nanorings Designed by Accurate Control of Glutathione S-Transferase Self-Assembly},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {135},
	number = {30},
	year = {2013},
	month = {JUL 31},
	pages = {10966-10969},
	abstract = {Protein self-assembly into exquisite, complex, yet highly ordered architectures represents the supreme wisdom of nature. However, precise manipulation of protein self-assembly behavior in vitro is a great challenge. Here we report that by taking advantage of the cooperation of metal-ion-chelating interactions and nonspecific protein protein interactions, we achieved accurate control of the orientation of proteins and their self-assembly into protein nanorings. As a building block, we utilized the C-2-symmetric protein sjGST-2His, a variant of glutathione S-transferase from Schistosoma japonicum having two properly oriented His metal-chelating sites on the surface. Through synergic metal-coordination and non-covalent interactions, sjGST-2His self-assembled in a fixed bending manner to form highly ordered protein nanorings. The diameters of the nanorings can be regulated by tuning the strength of the non-covalent interaction network between sjGST-2His interfaces through variation of the ionic strength of the solution. This work provides a de novo design strategy that can be applied in the construction of novel protein superstructures.},
	issn = {0002-7863},
	doi = {10.1021/ja405519s},
	author = {Bai, Yushi and Luo, Quan and Zhang, Wei and Miao, Lu and Xu, Jiayun and Li, Hongbin and Liu, Junqiu}
}
