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Volumn 319, Issue 2, 2002, Pages 541-554

The effects of ionic strength on protein stability: The cold shock protein family

Author keywords

Cold shock proteins; Electrostatics; Protein folding; Salt effects; Thermophilic proteins

Indexed keywords

COLD SHOCK PROTEIN; MUTANT PROTEIN; SODIUM CHLORIDE;

EID: 0036303785     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00259-0     Document Type: Article
Times cited : (158)

References (45)
  • 5
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting poly-electrolyte effects, Hofmeister effects, and osmotic effects of salts
    • (1998) Advan. Protein Chem. , vol.51 , pp. 281-353
    • Record M.T., Jr.1    Zhang, W.2    Anderson, C.F.3
  • 6
    • 0009940455 scopus 로고
    • Neutral salts. The generality of their effects on the stability of macromolecular conformations
    • (1964) Science , vol.145 , pp. 577-580
    • Von Hippel, P.H.1    Wong, K.Y.2
  • 12
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic, and extremely thermophilic protein subunits: Results of a comprehensive survey
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2
  • 15
  • 23
    • 0033544710 scopus 로고    scopus 로고
    • Realistic modeling of the denatured states of proteins allows accurate calculations of the pH dependence of protein stability
    • (1999) J. Mol. Biol. , vol.294 , pp. 1051-1062
    • Elcock, A.H.1
  • 37
    • 0028361968 scopus 로고
    • Structural origins of pH and ionic strength effects on protein stability. Acid denaturation of sperm whale apomyoglobin
    • (1994) J. Mol. Biol. , vol.237 , pp. 602-614
    • Yang, A.S.1    Honig, B.2
  • 41
    • 0028180523 scopus 로고
    • Application of scaled particle theory to model the hydrophobic effect: Implications for molecular association and protein stability
    • (1994) Protein Eng. , vol.7 , pp. 371-383
    • Jackson, R.M.1    Sternberg, M.J.2
  • 42
    • 0027980588 scopus 로고
    • Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: Evidence for residual electrostatic interactions in the acid/thermally denatured state
    • (1994) Biochemistry , vol.33 , pp. 8826-8832
    • Oliveberg, M.1    Vuilleumier, S.2    Fersht, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.