메뉴 건너뛰기




Volumn 46, Issue 35, 2007, Pages 9911-9919

Energetics of the native energy landscape of a two-domain calcium sensor protein: Distinct folding features of the two domains

Author keywords

[No Author keywords available]

Indexed keywords

BIOSENSORS; CARBON; HYDROGEN; POSITIVE IONS; THERMODYNAMICS;

EID: 34548510353     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700477h     Document Type: Article
Times cited : (10)

References (55)
  • 2
    • 33644847375 scopus 로고    scopus 로고
    • 2+: Molecular determinants and functional consequences
    • 2+: Molecular determinants and functional consequences, Physiol. Rev. 86, 369-408.
    • (2006) Physiol. Rev , vol.86 , pp. 369-408
    • Rizzuto, R.1    Pozzan, T.2
  • 4
    • 4444361538 scopus 로고    scopus 로고
    • Calcium-dependent regulation of secretion in biliary epithelial cells: The role of apamin-sensitive SK channels
    • Feranchak, A. P., Doctor, R. B., Troetsch, M., Brookman, K., Johnson, S. M., and Fitz, J. G. (2004) Calcium-dependent regulation of secretion in biliary epithelial cells: The role of apamin-sensitive SK channels, Gastroenterology 127, 903-913.
    • (2004) Gastroenterology , vol.127 , pp. 903-913
    • Feranchak, A.P.1    Doctor, R.B.2    Troetsch, M.3    Brookman, K.4    Johnson, S.M.5    Fitz, J.G.6
  • 6
    • 0032531818 scopus 로고    scopus 로고
    • Calcium: A life and death signal
    • Berridge, M. J., Bootman, M. D., and Lipp, P. (1998) Calcium: A life and death signal, Nature 395, 645-648.
    • (1998) Nature , vol.395 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 7
    • 0031238838 scopus 로고    scopus 로고
    • Differential role of calcium in tumour necrosis factor-mediated apoptosis and secretion of granulocyte-macrophage colony-stimulating factor in a T cell hybridoma
    • Denecker, G., Vandenabeele, P., Grooten, J., Penning, L. C., Declercq, W., Beyaert, R., Buurman, W. A., and Fiers, W. (1997) Differential role of calcium in tumour necrosis factor-mediated apoptosis and secretion of granulocyte-macrophage colony-stimulating factor in a T cell hybridoma, Cytokine 9, 631-638.
    • (1997) Cytokine , vol.9 , pp. 631-638
    • Denecker, G.1    Vandenabeele, P.2    Grooten, J.3    Penning, L.C.4    Declercq, W.5    Beyaert, R.6    Buurman, W.A.7    Fiers, W.8
  • 8
    • 0027161507 scopus 로고
    • Calcium signaling in the brain
    • Heizmann, C. W. (1993) Calcium signaling in the brain, Acta Neurobiol. Exp. 53, 15-23.
    • (1993) Acta Neurobiol. Exp , vol.53 , pp. 15-23
    • Heizmann, C.W.1
  • 9
    • 0025473993 scopus 로고
    • Internal calcium-binding proteins
    • Heizmann, C. W., and Schafer, B. W. (1990) Internal calcium-binding proteins, Semin. Cell Biol. 1, 277-282.
    • (1990) Semin. Cell Biol , vol.1 , pp. 277-282
    • Heizmann, C.W.1    Schafer, B.W.2
  • 10
  • 11
    • 0035107931 scopus 로고    scopus 로고
    • Solvation energetics and conformational change in EF-hand proteins
    • Ababou, A., and Desjarlais, J. R. (2001) Solvation energetics and conformational change in EF-hand proteins, Protein Sci. 10, 301-312.
    • (2001) Protein Sci , vol.10 , pp. 301-312
    • Ababou, A.1    Desjarlais, J.R.2
  • 13
    • 0026934952 scopus 로고
    • Calcium-binding proteins'. Basic concepts and clinical implications
    • Heizmann, C. W. (1992) Calcium-binding proteins'. Basic concepts and clinical implications, Gen. Physiol. Biophys. 11, 411-425.
    • (1992) Gen. Physiol. Biophys , vol.11 , pp. 411-425
    • Heizmann, C.W.1
  • 14
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein. II. Structure determination and general description
    • Kretsinger, R. H., and Nockolds, C. E. (1973) Carp muscle calcium-binding protein. II. Structure determination and general description, J. Biol. Chem. 248, 3313-3326.
    • (1973) J. Biol. Chem , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 15
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium-binding proteins
    • Strynadka, N. C., and James, M. N. (1989) Crystal structures of the helix-loop-helix calcium-binding proteins, Annu. Rev. Biochem. 58, 951-998.
    • (1989) Annu. Rev. Biochem , vol.58 , pp. 951-998
    • Strynadka, N.C.1    James, M.N.2
  • 17
    • 25144522326 scopus 로고    scopus 로고
    • P1CK1 is a calcium-sensor for NMDA-induced AMPA receptor trafficking
    • Hanley, J. G., and Henley, J. M. (2005) P1CK1 is a calcium-sensor for NMDA-induced AMPA receptor trafficking, EMBO J. 24, 3266-3278.
    • (2005) EMBO J , vol.24 , pp. 3266-3278
    • Hanley, J.G.1    Henley, J.M.2
  • 21
    • 23944462922 scopus 로고    scopus 로고
    • The concentrations of calcium buffering proteins in mammalian cochlear hair cells
    • Hackney, C. M., Mahendrasingam, S., Penn, A., and Fettiplace, R. (2005) The concentrations of calcium buffering proteins in mammalian cochlear hair cells, J. Neurosci. 25, 7867-7875.
    • (2005) J. Neurosci , vol.25 , pp. 7867-7875
    • Hackney, C.M.1    Mahendrasingam, S.2    Penn, A.3    Fettiplace, R.4
  • 25
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A., and Chan, H. S. (1997) From Levinthal to pathways to funnels, Nat. Struct. Biol. 4, 10-19.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 26
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: Bringing together theory and experiment
    • Dobson, C. M., and Karplus, M. (1999) The fundamentals of protein folding: Bringing together theory and experiment, Curr. Opin. Struct. Biol. 9, 92-101.
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 27
    • 16244419001 scopus 로고    scopus 로고
    • Elucidation of the protein folding landscape by NMR
    • Dyson, H. J., and Wright, P. E. (2005) Elucidation of the protein folding landscape by NMR, Methods Enzymol. 394, 299-321.
    • (2005) Methods Enzymol , vol.394 , pp. 299-321
    • Dyson, H.J.1    Wright, P.E.2
  • 28
    • 0038581260 scopus 로고    scopus 로고
    • Hidden intermediates and levinthal paradox in the folding of small proteins
    • Bai, Y. (2003) Hidden intermediates and levinthal paradox in the folding of small proteins, Biochem. Biophys. Res. Commun. 305, 785-788.
    • (2003) Biochem. Biophys. Res. Commun , vol.305 , pp. 785-788
    • Bai, Y.1
  • 29
    • 0032707706 scopus 로고    scopus 로고
    • The energetics of T4 lysozyme reveal a hierarchy of conformations
    • Llinas, M., Gillespie, B., Dahlquist, F. W., and Marqusee, S. (1999) The energetics of T4 lysozyme reveal a hierarchy of conformations, Nat. Struct. Biol. 6, 1072-1078.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 1072-1078
    • Llinas, M.1    Gillespie, B.2    Dahlquist, F.W.3    Marqusee, S.4
  • 30
    • 0033778161 scopus 로고    scopus 로고
    • Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange
    • Mayne, L., and Englander, S. W. (2000) Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange, Protein Sci. 9, 1873-1877.
    • (2000) Protein Sci , vol.9 , pp. 1873-1877
    • Mayne, L.1    Englander, S.W.2
  • 31
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson, S. E. (1998) How do small single-domain proteins fold? Folding Des. 3, R81-R91.
    • (1998) Folding Des , vol.3
    • Jackson, S.E.1
  • 32
    • 33645217096 scopus 로고    scopus 로고
    • The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals nonproductive misfolded intermediates
    • Bollen, Y. J., Kamphuis, M. B., and van Mierlo, C. P. (2006) The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals nonproductive misfolded intermediates, Proc. Natl. Acad. Sci. U.S.A. 103, 4095-4100.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 4095-4100
    • Bollen, Y.J.1    Kamphuis, M.B.2    van Mierlo, C.P.3
  • 33
    • 0033871781 scopus 로고    scopus 로고
    • Protein folding intermediates and pathways studied by hydrogen exchange
    • Englander, S. W. (2000) Protein folding intermediates and pathways studied by hydrogen exchange, Annu. Rev. Biophys. Biomol. Struct. 29, 213-238.
    • (2000) Annu. Rev. Biophys. Biomol. Struct , vol.29 , pp. 213-238
    • Englander, S.W.1
  • 35
    • 3342993181 scopus 로고    scopus 로고
    • Hydrogen exchange methods to study protein folding
    • Krishna, M. M., Hoang, L., Lin, Y., and Englander, S. W. (2004) Hydrogen exchange methods to study protein folding, Methods 34, 51-64.
    • (2004) Methods , vol.34 , pp. 51-64
    • Krishna, M.M.1    Hoang, L.2    Lin, Y.3    Englander, S.W.4
  • 36
    • 0030840017 scopus 로고    scopus 로고
    • Microsecond protein folding kinetics from native-state hydrogen exchange
    • Arlington, C. B., and Robertson, A. D. (1997) Microsecond protein folding kinetics from native-state hydrogen exchange, Biochemistry 36, 8686-8691.
    • (1997) Biochemistry , vol.36 , pp. 8686-8691
    • Arlington, C.B.1    Robertson, A.D.2
  • 37
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., Sosnick, T. R., Mayne, L., and Englander, S. W. (1995) Protein folding intermediates: Native-state hydrogen exchange, Science 269, 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 39
    • 0036408312 scopus 로고    scopus 로고
    • Thermodynamic and kinetic exploration of the energy landscape of Borrelia burgdorferi OspA by native-state hydrogen exchange
    • Yan, S., Kennedy, S. D., and Koide, S. (2002) Thermodynamic and kinetic exploration of the energy landscape of Borrelia burgdorferi OspA by native-state hydrogen exchange, J. Mol. Biol. 323, 363-375.
    • (2002) J. Mol. Biol , vol.323 , pp. 363-375
    • Yan, S.1    Kennedy, S.D.2    Koide, S.3
  • 40
    • 0029746061 scopus 로고    scopus 로고
    • Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
    • Chamberlain, A. K., Handel, T. M., and Marqusee, S. (1996) Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH, Nat. Struct. Biol. 3, 782-787.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 782-787
    • Chamberlain, A.K.1    Handel, T.M.2    Marqusee, S.3
  • 42
    • 0035807933 scopus 로고    scopus 로고
    • NMR derived solution structure of an EF-hand calcium-binding protein from Entamoeba Histolytica
    • Atreya, H. S., Sahu, S. C., Bhattacharya, A., Chary, K. V., and Govil, G. (2001) NMR derived solution structure of an EF-hand calcium-binding protein from Entamoeba Histolytica, Biochemistry 40, 14392-14403.
    • (2001) Biochemistry , vol.40 , pp. 14392-14403
    • Atreya, H.S.1    Sahu, S.C.2    Bhattacharya, A.3    Chary, K.V.4    Govil, G.5
  • 43
    • 23944454829 scopus 로고    scopus 로고
    • Structural characterization of the apo form of a calcium binding protein from Entamoeba histolytica by hydrogen exchange and its folding to the holo state
    • Mukherjee, S., Kuchroo, K., and Chary, K. V. (2005) Structural characterization of the apo form of a calcium binding protein from Entamoeba histolytica by hydrogen exchange and its folding to the holo state, Biochemistry 44, 11636-11645.
    • (2005) Biochemistry , vol.44 , pp. 11636-11645
    • Mukherjee, S.1    Kuchroo, K.2    Chary, K.V.3
  • 44
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A., and Nielsen, S. O. (1966) Hydrogen exchange in proteins, Adv. Protein Chem. 21, 287-386.
    • (1966) Adv. Protein Chem , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 46
    • 0032885077 scopus 로고    scopus 로고
    • Secondary structure of a calcium binding protein (CaBP) from Entamoeba histolytica
    • Sahu, S. C., Bhattacharya, A., Chary, K. V., and Govil, G. (1999) Secondary structure of a calcium binding protein (CaBP) from Entamoeba histolytica, FEBS Lett. 459, 51-56.
    • (1999) FEBS Lett , vol.459 , pp. 51-56
    • Sahu, S.C.1    Bhattacharya, A.2    Chary, K.V.3    Govil, G.4
  • 47
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants, Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 48
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity, J. Am. Chem. Soc. 114, 10663-10665.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 49
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J. S., Mayne, L., and Englander, S. W. (1993) Primary structure effects on peptide group hydrogen exchange, Proteins 17, 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 52
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou, P. Y., and Fasman, G. D. (1978) Empirical predictions of protein conformation, Annu. Rev. Biochem. 47, 251-276.
    • (1978) Annu. Rev. Biochem , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 53
    • 0037174849 scopus 로고    scopus 로고
    • Thermal unfolding of soybean peroxidase. Appropriate high denaturant concentrations induce cooperativity allowing the correct measurement of thermodynamic parameters
    • Kamal, J. K., Nazeerunnisa, M., and Behere, D. V. (2002) Thermal unfolding of soybean peroxidase. Appropriate high denaturant concentrations induce cooperativity allowing the correct measurement of thermodynamic parameters, J. Biol Chem. 277, 40717-40721.
    • (2002) J. Biol Chem , vol.277 , pp. 40717-40721
    • Kamal, J.K.1    Nazeerunnisa, M.2    Behere, D.V.3
  • 54
    • 0032545169 scopus 로고    scopus 로고
    • Characterisation of low free-energy excited states of folded proteins
    • Baxter, N. J., Hosszu, L. L., Waltho, J. P., and Williamson, M. P. (1998) Characterisation of low free-energy excited states of folded proteins, J. Mol Biol 284, 1625-1639.
    • (1998) J. Mol Biol , vol.284 , pp. 1625-1639
    • Baxter, N.J.1    Hosszu, L.L.2    Waltho, J.P.3    Williamson, M.P.4
  • 55
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wuthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures, J. Mol Graphics 14, 32-51.
    • (1996) J. Mol Graphics , vol.14 , pp. 32-51
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.