Unique Features of Halophilic Proteins

Curr Protein Pept Sci. 2017;18(1):65-71. doi: 10.2174/1389203717666160617111140.


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.

Publication types

  • Review

MeSH terms

  • Amino Acids
  • Archaeal Proteins / chemistry*
  • Bacterial Proteins / chemistry*
  • Hydrophobic and Hydrophilic Interactions
  • Intrinsically Disordered Proteins / chemistry
  • Protein Aggregates
  • Protein Folding
  • Salinity
  • Solubility
  • Temperature


  • Amino Acids
  • Archaeal Proteins
  • Bacterial Proteins
  • Intrinsically Disordered Proteins
  • Protein Aggregates