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Rui Yamaguchi
Department Kumamoto Health Science University Department of Medical Technology, Faculty of Health Science Kumamoto Health Science University Graduate School Division of Health Sciences, Graduate School of Health Sciences Position Associate Professor |
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| Language | English |
| Publication Date | 2017/01 |
| Type | |
| Peer Review | Peer reviewed |
| Title | Unique features of halopjilic proteins |
| Contribution Type | |
| Journal | Curr Protein Pept Sci. |
| Journal Type | Another Country |
| Volume, Issue, Page | 18,pp.65-71 |
| Total page number | 6 |
| Author and coauthor | Arakawa T,Yamaguchi R, Tokunaga H, Tokunaga M. |
| Details | Proteins from moderate and extreme halophiles have unique characteristics. They are highly acidic and hydrophilic, similar to intrinsically disordered proteins. These characteristics make the halophilic proteins soluble in water and fold reversibly. In addition to reversible folding, the rate of refolding of halophilic proteins from denatured structure is generally slow, often taking several days, for example, for extremely halophilic proteins. This slow folding rate makes the halophilic proteins a novel model system for folding mechanism analysis. High solubility and reversible folding also make the halophilic proteins excellent fusion partners for soluble expression of recombinant proteins. |