Unique Features of Halophilic Proteins

Title:Unique Features of Halophilic Proteins

Volume: 18 Issue: 1

Author(s): Tsutomu Arakawa, Rui Yamaguchi, Hiroko Tokunaga and Masao Tokunaga

Affiliation:

Keywords: Halophile, slow folding, reversibility, solubility, aggregation, fusion partner.

Abstract: 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.

Cite this article as:

Arakawa Tsutomu, Yamaguchi Rui, Tokunaga Hiroko and Tokunaga Masao, Unique Features of Halophilic Proteins, Current Protein & Peptide Science 2017; 18 (1) . https://dx.doi.org/10.2174/1389203717666160617111140