Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins

Protein and Peptide Letters

Volumn 11, Issue 2, 2004, Pages 125-132

  Arakawa, Tsutomu ^a   Tokunaga, Masao ^b  

^a ALLIANCE PROTEIN LABORATORIES   (United States)

^b KAGOSHIMA UNIVERSITY   (Japan)

Author keywords

Charge shielding; Halophilic; Nucleoside diphosphate kinase; Refolding; Salt

Indexed keywords

INORGANIC SALT; NUCLEOSIDE DIPHOSPHATE KINASE;

CHEMISTRY; ELECTRICITY; ENZYME STABILITY; ENZYMOLOGY; HALOBACTERIUM SALINARUM; HYDROPHOBICITY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; REVIEW; THERMODYNAMICS;

ELECTROSTATICS; ENZYME STABILITY; HALOBACTERIUM SALINARUM; HYDROPHOBICITY; NUCLEOSIDE-DIPHOSPHATE KINASE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SALTS; THERMODYNAMICS;

HALOBACTERIUM SALINARUM;

EID: 1942521068     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/0929866043478220     Document Type: Review

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