메뉴 건너뛰기




Volumn 79, Issue 4, 2000, Pages 2171-2177

Cation-binding sites of subtilisin carlsberg probed with Eu(III) luminescence

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; EUROPIUM; SUBTILISIN;

EID: 0033799270     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76465-4     Document Type: Article
Times cited : (3)

References (7)
  • 1
    • 0041322026 scopus 로고    scopus 로고
    • Non-radiative deactivation of the excited states of europium, terbium and ytterbium complexes by proximate energy-matched OH, NH and CH oscillators: An improved luminescence method for establishing solution hydration states
    • Beeby, A., I. M. Clarkson, R. S. Dickins, S. Faulkner, D. Parker, L. Royle, A. S. de Sousa, J. A. G. Williams, and M. Woods. 1999. Non-radiative deactivation of the excited states of europium, terbium and ytterbium complexes by proximate energy-matched OH, NH and CH oscillators: an improved luminescence method for establishing solution hydration states. J. Chem. Soc. Perkin Trans. 2:493-503.
    • (1999) J. Chem. Soc. Perkin Trans. 2 , pp. 493-503
    • Beeby, A.1    Clarkson, I.M.2    Dickins, R.S.3    Faulkner, S.4    Parker, D.5    Royle, L.6    De Sousa, A.S.7    Williams, J.A.G.8    Woods, M.9
  • 2
    • 0023643147 scopus 로고
    • The high-resolution x-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis
    • Bode, W., E. Papamokos, and D. Musil. 1987. The high-resolution x-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Eur. J. Biochem. 166:673-692.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 3
    • 0029560442 scopus 로고
    • Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy. Evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility
    • Broos, J., A. J. W. G. Visser, J. F. J. Engbersen, W. Verboom, A. van Hoek, and D. N. Reinhoudt. 1995. Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy. Evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility. J. Am. Chem. Soc. 117:12657-12663.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 12657-12663
    • Broos, J.1    Visser, A.J.W.G.2    Engbersen, J.F.J.3    Verboom, W.4    Van Hoek, A.5    Reinhoudt, D.N.6
  • 6
    • 0024280501 scopus 로고
    • Dissecting the catalytic triad of a serine protease
    • Carter, P., and J. A. Wells. 1988. Dissecting the catalytic triad of a serine protease. Nature. 332:564-568.
    • (1988) Nature , vol.332 , pp. 564-568
    • Carter, P.1    Wells, J.A.2
  • 7
    • 0017075046 scopus 로고
    • Role of bound calcium ions in thermostable, proteolytic enzymes. Separation of intrinsic and calcium ion contributions to the kinetic thermal stability
    • Voordouw, G., C. Milo, and R. S. Roche. 1976. Role of bound calcium ions in thermostable, proteolytic enzymes. Separation of intrinsic and calcium ion contributions to the kinetic thermal stability. Biochemistry. 15:3716-3724.
    • (1976) Biochemistry , vol.15 , pp. 3716-3724
    • Voordouw, G.1    Milo, C.2    Roche, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.