메뉴 건너뛰기




Volumn 35, Issue 1-2, 2004, Pages 11-13

Modeling techniques for analysing conformational transitions in hemocyanins by small-angle scattering of X-rays and neutrons

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 1242277891     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micron.2003.10.004     Document Type: Conference Paper
Times cited : (3)

References (10)
  • 1
    • 0031807272 scopus 로고    scopus 로고
    • Low-resolution structures of proteins in solution retrieved from X-ray scattering with a genetic algorithm
    • Chacon P., Moran F., Diaz J.F., Pantos E., Andreu J.M. Low-resolution structures of proteins in solution retrieved from X-ray scattering with a genetic algorithm. Biophys. J. 74:1998;2760-2775.
    • (1998) Biophys. J. , vol.74 , pp. 2760-2775
    • Chacon, P.1    Moran, F.2    Diaz, J.F.3    Pantos, E.4    Andreu, J.M.5
  • 2
    • 0030590489 scopus 로고    scopus 로고
    • Small-angle X-ray scattering reveals differences between the quaternary structures of oxygenated and deoxygenated tarantula hemocyanin
    • Decker H., Hartmann H., Sterner R., Schwarz E., Pilz I. Small-angle X-ray scattering reveals differences between the quaternary structures of oxygenated and deoxygenated tarantula hemocyanin. FEBS Lett. 393:1996;226-230.
    • (1996) FEBS Lett. , vol.393 , pp. 226-230
    • Decker, H.1    Hartmann, H.2    Sterner, R.3    Schwarz, E.4    Pilz, I.5
  • 3
    • 0034778181 scopus 로고    scopus 로고
    • Small-angle neutron scattering reveals an oxygen-dependent conformational change of the immunogen keyhole limpet hemocyanin type 1 (KLH1)
    • Hartmann H., Bongers A., Decker H. Small-angle neutron scattering reveals an oxygen-dependent conformational change of the immunogen keyhole limpet hemocyanin type 1 (KLH1). Eur. Biophys. J. 30:2001;471-475.
    • (2001) Eur. Biophys. J. , vol.30 , pp. 471-475
    • Hartmann, H.1    Bongers, A.2    Decker, H.3
  • 4
    • 0035827704 scopus 로고    scopus 로고
    • The allosteric effector L-lactate induces a conformational change of 2×6-meric lobster hemocyanin in the oxy state as revealed by small angle X-ray scattering
    • Hartmann H., Lohkamp B., Hellmann N., Decker H. The allosteric effector L-lactate induces a conformational change of 2×6-meric lobster hemocyanin in the oxy state as revealed by small angle X-ray scattering. J. Biol. Chem. 276:2001;19954-19958.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19954-19958
    • Hartmann, H.1    Lohkamp, B.2    Hellmann, N.3    Decker, H.4
  • 5
    • 0037121459 scopus 로고    scopus 로고
    • All hierarchical levels are involved in conformational transitions of the 4×6-meric tarantula hemocyanin upon oxygenation
    • Hartmann H., Decker H. All hierarchical levels are involved in conformational transitions of the 4×6-meric tarantula hemocyanin upon oxygenation. Biochim. Biophys. Acta. 1601:2002;132-137.
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 132-137
    • Hartmann, H.1    Decker, H.2
  • 6
    • 1242293870 scopus 로고    scopus 로고
    • Small-angle scattering techniques for analysing conformational transitions in hemocyanins
    • J.M. Holt, M.L. Johnson, & G.K. Ackers. London: Academic Press. in press
    • Hartmann H., Decker H. Small-angle scattering techniques for analysing conformational transitions in hemocyanins. Holt J.M., Johnson M.L., Ackers G.K. Methods in Enzymology. 2003;Academic Press, London. in press.
    • (2003) Methods in Enzymology
    • Hartmann, H.1    Decker, H.2
  • 7
    • 1242338977 scopus 로고    scopus 로고
    • Small-angle X-ray scattering based 3D reconstruction of the immunogen KLH1 reveals different oxygen dependent conformations
    • in press
    • Hartmann, H., Bongers, A., Decker, H., 2004. Small-angle X-ray scattering based 3D reconstruction of the immunogen KLH1 reveals different oxygen dependent conformations. J. Biol. Chem., in press.
    • (2004) J. Biol. Chem.
    • Hartmann, H.1    Bongers, A.2    Decker, H.3
  • 8
    • 0027529265 scopus 로고
    • Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 a resolution: Clues for a mechanism for allosteric regulation
    • Hazes B., Magnus K.A., Bonaventura C., Bonaventura J., Dauter Z., Kalk K.H., Hol W.G. Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation. Protein Sci. 2:1993;597-619.
    • (1993) Protein Sci. , vol.2 , pp. 597-619
    • Hazes, B.1    Magnus, K.A.2    Bonaventura, C.3    Bonaventura, J.4    Dauter, Z.5    Kalk, K.H.6    Hol, W.G.7
  • 9
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76:1999;2879-2886.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 10
    • 0036816606 scopus 로고    scopus 로고
    • Advances in structure analysis using small-angle scattering in solution
    • Svergun D.I., Koch M.H. Advances in structure analysis using small-angle scattering in solution. Curr. Opin. Struct. Biol. 12:2002;654-660.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 654-660
    • Svergun, D.I.1    Koch, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.