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Volumn 11, Issue 7, 2002, Pages 1681-1686

Modeling of denatured state for calculation of the electrostatic contribution to protein stability

Author keywords

Denatured state; Electrostatic interactions; Free energy; PH dependence; Proteins

Indexed keywords

RIBOSOME PROTEIN; BACILLUS AMYLOLIQUEFACIENS RIBONUCLEASE; PROTEIN; RIBONUCLEASE; RIBOSOMAL PROTEIN L9;

EID: 0036081435     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.4690102     Document Type: Article
Times cited : (27)

References (24)
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  • 6
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  • 7
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  • 9
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    • a values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions
    • (1999) Biochemistry , vol.38 , pp. 4896-4903
    • Kuhlman, B.1    Luisi, D.L.2    Young, P.3    Raleigh, D.P.4
  • 11
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    • pH-dependent interactions and the stability and folding kinetics of the N-terminal domain of L9. Electrostatic interactions are only weakly formed in the transition state of folding
    • (2000) J. Mol. Biol. , vol.299 , pp. 1091-1100
    • Luisi, D.L.1    Raleigh, D.P.2
  • 14
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    • Thermodynamic study of the acid denaturation of bamase and its dependence on ionic strength: Evidence for residual electrostatic interactions in the acid/thermal denatured state
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  • 23
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    • Simplified methods for pK(a) and acid pH-dependent stability estimation in proteins: Removing dielectric and counterion boundaries
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  • 24
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    • Structural origin of pH and ionic strength effects on protein stability. Acid denaturation of sperm whale apomyoglobin
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    • Yang, A.-S.1    Honig, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.