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Volumn 309, Issue 5, 2001, Pages 1165-1175

The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins

Author keywords

Folding intermediate; m values; pH effects; pKa; Staphylococcal nuclease

Indexed keywords

BACTERIAL ENZYME; GUANIDINE; NUCLEASE; PROTEIN; UREA;

EID: 0035933338     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4726     Document Type: Article
Times cited : (42)

References (31)
  • 2
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 5
    • 0031808804 scopus 로고    scopus 로고
    • Chemical denaturation: Potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption
    • (1998) Biophys. J. , vol.75 , pp. 484-492
    • Soulages, J.L.1
  • 11
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 13
    • 0033600572 scopus 로고    scopus 로고
    • The peculiar nature of the guanidine hydrochloride-induced two-state denaturation of staphylococcal nuclease: A calorimetric study
    • (1999) Biochemistry , vol.38 , pp. 11216-11222
    • Yang, M.1    Liu, D.2    Bolen, D.W.3
  • 14
    • 0032558991 scopus 로고    scopus 로고
    • Monitoring the sizes of denatured ensembles of staphylococcal nuclease proteins: Implications regarding m values, intermediates, and thermodynamics
    • (1998) Biochemistry , vol.37 , pp. 18010-18017
    • Baskakov, I.V.1    Bolen, D.W.2
  • 16
    • 0028960492 scopus 로고
    • How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 17
    • 4244124315 scopus 로고    scopus 로고
    • Investigations of denatured state structurual and m-value effects in staphylococcal nuclease
    • PhD dissertation, The Johns Hopkins University, USA
    • (1999)
    • Wrable, J.1
  • 20
    • 0028856228 scopus 로고
    • The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions by NMR and CD spectroscopy
    • (1995) Biochemistry , vol.34 , pp. 15895-15905
    • Wang, Y.1    Shortle, D.2
  • 21
  • 28
    • 0031038733 scopus 로고    scopus 로고
    • Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nudease and two of its variants
    • (1997) Biochemistry , vol.36 , pp. 1129-1140
    • Ionescu, R.M.1    Eftink, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.