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Volumn 44, Issue 31, 2005, Pages 10732-10740

Linear free-energy analysis of mercury(II) and cadmium(II) binding to three-stranded coiled coils

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CADMIUM COMPOUNDS; DISSOCIATION; FREE ENERGY; MOLECULAR STRUCTURE; PERTURBATION TECHNIQUES; PROTEINS; RATE CONSTANTS; SYNTHESIS (CHEMICAL);

EID: 23244435277     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0506674     Document Type: Article
Times cited : (51)

References (34)
  • 2
    • 0000933784 scopus 로고
    • A consensus Zinc finger peptide: Design, high affinity metal-binding, a pH-dependent structure, and His to Cys sequence variation
    • Krizek, B. A., Amann, B. T., Kilfoil, V. J., Merkle, D. L., and Berg, J. M. (1991) A consensus Zinc finger peptide: Design, high affinity metal-binding, a pH-dependent structure, and His to Cys sequence variation, J. Am. Chem. Soc. 113, 4518-4523.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4518-4523
    • Krizek, B.A.1    Amann, B.T.2    Kilfoil, V.J.3    Merkle, D.L.4    Berg, J.M.5
  • 4
    • 11944257538 scopus 로고
    • Secondary structure nucleation in peptides. Transition metal ion stabilized α-helices
    • Ghadiri, M. R., and Choi, C. (1990) Secondary structure nucleation in peptides. Transition metal ion stabilized α-helices, J. Am. Chem. Soc. 112, 1630-1632.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 1630-1632
    • Ghadiri, M.R.1    Choi, C.2
  • 5
    • 84989506919 scopus 로고
    • Design of an artificial four helix-bundle metalloprotein via a novel ruthenium-(II) assisted self-assembly process
    • Ghadiri, M. R., Soares, C., and Choi, C. (1992) Design of an artificial four helix-bundle metalloprotein via a novel ruthenium-(II) assisted self-assembly process, J. Am. Chem. Soc. 114, 4000-4002.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4000-4002
    • Ghadiri, M.R.1    Soares, C.2    Choi, C.3
  • 6
    • 0028103524 scopus 로고
    • Dynamic structure and potential-energy surface of a 3-helix bundle protein
    • Lieberman, M., Tabet, M., and Sasaki, T. (1994) Dynamic structure and potential-energy surface of a 3-helix bundle protein, J. Am. Chem. Soc. 116, 5035-5044.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5035-5044
    • Lieberman, M.1    Tabet, M.2    Sasaki, T.3
  • 7
    • 0032542575 scopus 로고    scopus 로고
    • Metal ion induced folding of a de novo designed coiled-coil peptide
    • Kohn, W. D., Kay, C. M., Sykes, B. D., and Hodges, R. S. (1998) Metal ion induced folding of a de novo designed coiled-coil peptide, J. Am. Chem. Soc. 120, 1124-1132.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1124-1132
    • Kohn, W.D.1    Kay, C.M.2    Sykes, B.D.3    Hodges, R.S.4
  • 8
    • 0030828321 scopus 로고    scopus 로고
    • Electron transfer across a peptide-peptide interface within a designed metalloprotein
    • Ogawa, M. Y., and Kozlov, G. V. (1997) Electron transfer across a peptide-peptide interface within a designed metalloprotein, J. Am. Chem. Soc. 119, 8377-8378.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8377-8378
    • Ogawa, M.Y.1    Kozlov, G.V.2
  • 9
    • 0037438702 scopus 로고    scopus 로고
    • Photon-induced electron-transfer along α-helical and coiled coil metallopeptides
    • Federova, A., Chaudhari, A., and Ogawa, M. Y. (2002) Photon-induced electron-transfer along α-helical and coiled coil metallopeptides, J. Am. Chem. Soc. 125, 357-362.
    • (2002) J. Am. Chem. Soc. , vol.125 , pp. 357-362
    • Federova, A.1    Chaudhari, A.2    Ogawa, M.Y.3
  • 13
    • 0037055019 scopus 로고    scopus 로고
    • Comparison of the binding of cadmium(II), mercury(II), and arsenic(III) to the de now designed peptides TRI L12C and TRI L16C
    • Matzapetakis, M., Farrer, B. T., Weng, T.-C., Hemmingsen, L., Penner-Hahn, J. E., and Pecoraro, V. L. (2002) Comparison of the binding of cadmium(II), mercury(II), and arsenic(III) to the de now designed peptides TRI L12C and TRI L16C, J. Am. Chem. Soc. 124, 8042-8054.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8042-8054
    • Matzapetakis, M.1    Farrer, B.T.2    Weng, T.-C.3    Hemmingsen, L.4    Penner-Hahn, J.E.5    Pecoraro, V.L.6
  • 14
    • 0035807939 scopus 로고    scopus 로고
    • Thermodynamic model for the stabilization of trigonal thiolato mercury(II) in designed three-stranded coiled coils
    • Farrer, B. T., Harris, N. P., Balchus, K. E., and Pecoraro, V. L. (2001) Thermodynamic model for the stabilization of trigonal thiolato mercury(II) in designed three-stranded coiled coils, Biochemistry 40, 14696-14705.
    • (2001) Biochemistry , vol.40 , pp. 14696-14705
    • Farrer, B.T.1    Harris, N.P.2    Balchus, K.E.3    Pecoraro, V.L.4
  • 15
    • 10044289354 scopus 로고    scopus 로고
    • Understanding metalloprotein folding using a de novo design strategy
    • Ghosh, D., and Pecoraro, V. L. (2004) Understanding metalloprotein folding using a de novo design strategy, Inorg. Chem. 43, 7902-7915.
    • (2004) Inorg. Chem. , vol.43 , pp. 7902-7915
    • Ghosh, D.1    Pecoraro, V.L.2
  • 19
    • 0030445131 scopus 로고    scopus 로고
    • Thermodynamic analysis of a designed three-stranded coiled coil
    • Boice, J. A., Dieckmann, G. R., Degrado, W. F., and Fairman, R. (1996) Thermodynamic analysis of a designed three-stranded coiled coil, Biochemistry 35, 14480-14485.
    • (1996) Biochemistry , vol.35 , pp. 14480-14485
    • Boice, J.A.1    Dieckmann, G.R.2    Degrado, W.F.3    Fairman, R.4
  • 20
    • 8844265931 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of highly heterogeneous systems
    • Demeler, B., and van Holde, K. E. (2004) Sedimentation velocity analysis of highly heterogeneous systems, Anal. Biochem. 335, 279-288.
    • (2004) Anal. Biochem. , vol.335 , pp. 279-288
    • Demeler, B.1    Van Holde, K.E.2
  • 22
    • 0032584776 scopus 로고    scopus 로고
    • The role of protonation and metal chelation preferences in defining the properties of mercury-binding coiled coils
    • Dieckmann, G. R., McRorie, D. K., Lear, J. D., Sharp, K. A., DeGrado, W. F., and Pecoraro, V. L. (1998) The role of protonation and metal chelation preferences in defining the properties of mercury-binding coiled coils, J. Mol. Biol. 280, 897-912.
    • (1998) J. Mol. Biol. , vol.280 , pp. 897-912
    • Dieckmann, G.R.1    McRorie, D.K.2    Lear, J.D.3    Sharp, K.A.4    Degrado, W.F.5    Pecoraro, V.L.6
  • 23
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson, M. L., Correia, J. J., Yphantis, D. A., and Halvorson, H. R. (1981) Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques, Biophys. J. 36, 575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 24
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S. C., and von Hippel P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 25
    • 0031020113 scopus 로고    scopus 로고
    • Identification and interpretation of complexity in sedimentation velocity boundaries
    • Demeler, B., Saber, H., and Hansen, J. C. (1997) Identification and interpretation of complexity in sedimentation velocity boundaries, Biophys. J. 72, 397-407.
    • (1997) Biophys. J. , vol.72 , pp. 397-407
    • Demeler, B.1    Saber, H.2    Hansen, J.C.3
  • 28
    • 0024508489 scopus 로고
    • Transcriptional switching by the metalloregulatory merR protein: Initial characterization of DNA and mercury(II) binding activities
    • Shewchuk, L. M., Verdine, G. L., and Walsh, C. T. (1989) Transcriptional switching by the metalloregulatory merR protein: Initial characterization of DNA and mercury(II) binding activities, Biochemistry 28, 2331-2339.
    • (1989) Biochemistry , vol.28 , pp. 2331-2339
    • Shewchuk, L.M.1    Verdine, G.L.2    Walsh, C.T.3
  • 30
    • 0034722236 scopus 로고    scopus 로고
    • Arsenic stabilizes three-helix bundles in aqueous solution
    • Farrer, B., McClure, C., Penner-Hahn, J. E., and Pecoraro, V. L. (2000) Arsenic stabilizes three-helix bundles in aqueous solution, Inorg. Chem. 39, 5422-5423.
    • (2000) Inorg. Chem. , vol.39 , pp. 5422-5423
    • Farrer, B.1    McClure, C.2    Penner-Hahn, J.E.3    Pecoraro, V.L.4
  • 33
    • 0037802590 scopus 로고
    • Polarimetric and nuclear magnetic resonance studies of the complexation of mercury by thiols
    • Shoukry, M. H., Cheesman, B. V., and Rabenstein, D. L. (1988) Polarimetric and nuclear magnetic resonance studies of the complexation of mercury by thiols, Can. J. Chem. 66, 3184-3190.
    • (1988) Can. J. Chem. , vol.66 , pp. 3184-3190
    • Shoukry, M.H.1    Cheesman, B.V.2    Rabenstein, D.L.3
  • 34
    • 3342880704 scopus 로고    scopus 로고
    • Control of metal coordination number in de novo designed peptides through subtle sequence modifications
    • Lee, K.-H., Matzapetakis, M., Mitra, S., Marsh, E. N. G., and Pecoraro, V. L. (2004) Control of metal coordination number in de novo designed peptides through subtle sequence modifications, J. Am. Chem. Soc. 126, 9178-9179.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9178-9179
    • Lee, K.-H.1    Matzapetakis, M.2    Mitra, S.3    Marsh, E.N.G.4    Pecoraro, V.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.