Amyloid fibril formation in vitro from halophilic metal binding protein: Its high solubility and reversibility minimized formation of amorphous protein aggregations
Article first published online: 30 SEP 2013
© 2013 The Protein Society
Volume 22, Issue 11, pages 1582–1591, November 2013
How to Cite
Tokunaga, Y., Matsumoto, M., Tokunaga, M., Arakawa, T. and Sugimoto, Y. (2013), Amyloid fibril formation in vitro from halophilic metal binding protein: Its high solubility and reversibility minimized formation of amorphous protein aggregations. Protein Science, 22: 1582–1591. doi: 10.1002/pro.2359
- Issue published online: 21 OCT 2013
- Article first published online: 30 SEP 2013
- Accepted manuscript online: 29 AUG 2013 06:40AM EST
- Manuscript Accepted: 22 AUG 2013
- Manuscript Revised: 21 AUG 2013
Additional Supporting Information may be found in the online version of this article.
|pro2359-sup-0002-suppfig1.tif||1114K||Supporting Information Figure 1. Analysis of peptides involved in fibril formation.|
|pro2359-sup-0003-suppfig2.tif||50K||Supporting Information Figure 2. TOF-MS analysis of Peak A, B and C.|
|pro2359-sup-0004-supptable1.doc||30K||Supporting Information Table 1. Summary of peptides isolated from precipitated fibrils formed from His-HP incubated at pH2.0 and 58 oC.|
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