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Volumn 81, Issue 6, 2001, Pages 3489-3502

pH corrections and protein ionization in water/guanidinium chloride

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACID DERIVATIVE; CHYMOTRYPSIN A; GUANIDINE; NUCLEASE; RIBONUCLEASE A; SODIUM CHLORIDE; WATER;

EID: 0035193201     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)75980-2     Document Type: Article
Times cited : (43)

References (33)
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  • 8
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  • 19
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    • Protein denaturation with guanidinium chloride hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • (1994) Protein Sci. , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 20
    • 0014203499 scopus 로고
    • Acid-base titrations in concentrated guanidinium chloride hydrochloride. Dissociation constants of the guanidinium ion and of some amino acids
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 736-742
    • Nozaki, Y.1    Tanford, C.2
  • 21
    • 0014203395 scopus 로고
    • Proteins as random coils. II. Hydrogen ion titration curve of ribonuclease in 6 M guanidinium chloride hydrochloride
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 742-749
    • Nozaki, Y.1    Tanford, C.2
  • 22
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidinium chloride hydrochloride denaturation curves
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 27
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    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 28
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    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 32
    • 0034700307 scopus 로고    scopus 로고
    • pH dependence of stability of staphylococcal nuclease: Evidence of substantial electrostatic interactions in the denatured state
    • (2000) Biochemistry , vol.39 , pp. 14292-14304
    • Whitten, S.T.1    Garcia-Moreno, B.2
  • 33
    • 0028960492 scopus 로고
    • How valid are denaturant-induced unfolding free measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability
    • (1995) Biochemistry , vol.34 , pp. 3771-3779
    • Yao, M.1    Bolen, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.