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Volumn 52, Issue 2, 2005, Pages 477-483

A 2D-IR study of heat- and [13C]urea-induced denaturation of sarcoplasmic reticulum Ca2+-ATPase

Author keywords

2D IR; Heat induced denaturation; Sarcoplasmic reticulum; Urea induced denaturation

Indexed keywords


EID: 23644434417     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2005_3462     Document Type: Article
Times cited : (14)

References (37)
  • 3
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo JL, Muga A, Castresana J, Goni FM (1993) Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog Biophys Mol Biol 59: 23-56.
    • (1993) Prog Biophys Mol Biol , vol.59 , pp. 23-56
    • Arrondo, J.L.1    Muga, A.2    Castresana, J.3    Goni, F.M.4
  • 4
    • 0027987495 scopus 로고
    • Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy
    • Arrondo JL, Castresana J, Valpuesta JM, Goni FM (1994) Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy. Biochemistry 33: 11650-11655.
    • (1994) Biochemistry , vol.33 , pp. 11650-11655
    • Arrondo, J.L.1    Castresana, J.2    Valpuesta, J.M.3    Goni, F.M.4
  • 5
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo JL, Goñi FM (1999) Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog Biophys Mol Biol 72: 367-405.
    • (1999) Prog Biophys Mol Biol , vol.72 , pp. 367-405
    • Arrondo, J.L.1    Goñi, F.M.2
  • 7
    • 0028948157 scopus 로고
    • Surface-core relationships in human low density lipoprotein as studied by infrared spectroscopy
    • Bañuelos S, Arrondo JL, Goni FM, Pifat G (1995) Surface-core relationships in human low density lipoprotein as studied by infrared spectroscopy. J Biol Chem 270: 9192-9196.
    • (1995) J Biol Chem , vol.270 , pp. 9192-9196
    • Bañuelos, S.1    Arrondo, J.L.2    Goni, F.M.3    Pifat, G.4
  • 8
    • 0027940230 scopus 로고
    • (2+)-ATPase: Investigation of nucleotide binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy
    • (2+)-ATPase: investigation of nucleotide binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy. Biochim Biophys Acta 1194: 75-91.
    • (1994) Biochim Biophys Acta , vol.1194 , pp. 75-91
    • Barth, A.1    Kreutz, W.2    Mantele, W.3
  • 10
    • 0024320718 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum: A Fourier transform infrared spectroscopy (FTIR) study on the effects of dimethyl sulfoxide and urea
    • 2+-ATPase of sarcoplasmic reticulum: a Fourier transform infrared spectroscopy (FTIR) study on the effects of dimethyl sulfoxide and urea. Biochim Biophys Acta 983: 167-178.
    • (1989) Biochim Biophys Acta , vol.983 , pp. 167-178
    • Buchet, R.1    Jona, I.2    Martonosi, A.3
  • 11
    • 0035853068 scopus 로고    scopus 로고
    • Structure and interaction with membrane model systems of a peptide derived from the major epitope region of HIV protein gp41: Implications on viral fusion mechanism
    • Contreras LM, Aranda FJ, Gavilanes F, Gonzalez-Ros JM, Villalain J (2001) Structure and interaction with membrane model systems of a peptide derived from the major epitope region of HIV protein gp41: implications on viral fusion mechanism. Biochemistry 40: 3196-3207.
    • (2001) Biochemistry , vol.40 , pp. 3196-3207
    • Contreras, L.M.1    Aranda, F.J.2    Gavilanes, F.3    Gonzalez-Ros, J.M.4    Villalain, J.5
  • 12
    • 0029977715 scopus 로고    scopus 로고
    • The denaturation and degradation of stable enzymes at high temperatures
    • Daniel RM, Dines M, Petach HH (1996) The denaturation and degradation of stable enzymes at high temperatures. Biochem J 317: 1-11.
    • (1996) Biochem J , vol.317 , pp. 1-11
    • Daniel, R.M.1    Dines, M.2    Petach, H.H.3
  • 13
    • 0031807972 scopus 로고    scopus 로고
    • Topology of sarcoplasmic reticulum Ca2+-ATPase: An infrared study of thermal denaturation and limited proteolysis
    • Echabe I, Dornberger U, Prado A, Goni FM, Arrondo JL (1998) Topology of sarcoplasmic reticulum Ca2+-ATPase: an infrared study of thermal denaturation and limited proteolysis. Protein Sci 7: 1172-1179.
    • (1998) Protein Sci , vol.7 , pp. 1172-1179
    • Echabe, I.1    Dornberger, U.2    Prado, A.3    Goni, F.M.4    Arrondo, J.L.5
  • 14
    • 0033539558 scopus 로고    scopus 로고
    • Two-dimensional IR correlation spectroscopy: Sequential events in the unfolding process of the lambda cro-V55C repressor protein
    • Fabian H, Mantsch HH, Schultz CP (1999) Two-dimensional IR correlation spectroscopy: sequential events in the unfolding process of the lambda cro-V55C repressor protein. Proc Natl Acad Sci USA 96: 13153-13158.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13153-13158
    • Fabian, H.1    Mantsch, H.H.2    Schultz, C.P.3
  • 15
    • 4644293577 scopus 로고    scopus 로고
    • Conformation-dependent antibodies target diseases of protein misfolding
    • Glabe CG (2004) Conformation-dependent antibodies target diseases of protein misfolding. Trends Biochem Sci 29: 542-547.
    • (2004) Trends Biochem Sci , vol.29 , pp. 542-547
    • Glabe, C.G.1
  • 16
    • 2942687911 scopus 로고    scopus 로고
    • Methionine adenosyltransferase alpha-helix structure unfolds at lower temperatures than beta-sheet: A 2D-IR study
    • Iloro I, Chehin R, Goni FM, Pajares MA, Arrondo JL (2004) Methionine adenosyltransferase alpha-helix structure unfolds at lower temperatures than beta-sheet: a 2D-IR study. Biophys J 86: 3951-3958.
    • (2004) Biophys J , vol.86 , pp. 3951-3958
    • Iloro, I.1    Chehin, R.2    Goni, F.M.3    Pajares, M.A.4    Arrondo, J.L.5
  • 17
    • 0015759310 scopus 로고
    • Temperature-induced transitions of function and structure in sarcoplasmic reticulum membranes
    • Inesi G, Millman M, Eletr S (1973) Temperature-induced transitions of function and structure in sarcoplasmic reticulum membranes. J Mol Biol 81: 483-504.
    • (1973) J Mol Biol , vol.81 , pp. 483-504
    • Inesi, G.1    Millman, M.2    Eletr, S.3
  • 18
    • 11244260589 scopus 로고    scopus 로고
    • Monitoring protein folding at atomic resolution
    • Kumar TK, Yu C (2004) Monitoring protein folding at atomic resolution. Acc Chem Res 37: 929-936.
    • (2004) Acc Chem Res , vol.37 , pp. 929-936
    • Kumar, T.K.1    Yu, C.2
  • 19
    • 11844304103 scopus 로고    scopus 로고
    • Measurement of protein stability and protein denaturation in cells using differential scanning calorimetry
    • Lepock JR (2005) Measurement of protein stability and protein denaturation in cells using differential scanning calorimetry. Methods 35: 117-125.
    • (2005) Methods , vol.35 , pp. 117-125
    • Lepock, J.R.1
  • 21
    • 0030592166 scopus 로고    scopus 로고
    • Structure-function relationships in the Ca(2+)-ATPase of sarcoplasmic reticulum: Facts, speculations and questions for the future
    • Martonosi AN (1996) Structure-function relationships in the Ca(2+)-ATPase of sarcoplasmic reticulum: facts, speculations and questions for the future. Biochim Biophys Acta 1275: 111-117.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 111-117
    • Martonosi, A.N.1
  • 22
    • 0042381683 scopus 로고    scopus 로고
    • The structure of the Ca2+-ATPase of sarcoplasmic reticulum
    • Martonosi AN, Pikula S (2003) The structure of the Ca2+-ATPase of sarcoplasmic reticulum. Acta Biochim Polon 50: 337-365.
    • (2003) Acta Biochim Polon , vol.50 , pp. 337-365
    • Martonosi, A.N.1    Pikula, S.2
  • 23
    • 0033778161 scopus 로고    scopus 로고
    • Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange
    • Mayne L, Englander SW (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
  • 24
    • 0016378337 scopus 로고
    • Isolation of sarcoplasmic reticulum from skeletal muscle
    • Meissner G (1974) Isolation of sarcoplasmic reticulum from skeletal muscle. Methods Enzymol 31: 238-246.
    • (1974) Methods Enzymol , vol.31 , pp. 238-246
    • Meissner, G.1
  • 25
    • 0017114142 scopus 로고
    • Mechanism of ATP hydrolysis by sarcoplasmic reticulum and the role of phospholipids
    • Nakamura H, Jilka RL, Boland R, Martonosi AN (1976) Mechanism of ATP hydrolysis by sarcoplasmic reticulum and the role of phospholipids. J Biol Chem. 251: 5414-5423.
    • (1976) J Biol Chem , vol.251 , pp. 5414-5423
    • Nakamura, H.1    Jilka, R.L.2    Boland, R.3    Martonosi, A.N.4
  • 26
    • 0034957763 scopus 로고    scopus 로고
    • Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol
    • Paquet MJ, Laviolette M, Pezolet M, Auger M (2001) Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol. Biophys J 81: 305-312.
    • (2001) Biophys J , vol.81 , pp. 305-312
    • Paquet, M.J.1    Laviolette, M.2    Pezolet, M.3    Auger, M.4
  • 28
    • 0021111186 scopus 로고
    • Membrane-surfactant interactions. The effect of Triton X-100 on sarcoplasmic reticulum vesicles
    • Prado A, Arrondo JL, Villena A, Goni FM, Macarulla JM (1983) Membrane-surfactant interactions. The effect of Triton X-100 on sarcoplasmic reticulum vesicles. Biochim Biophys Acta 733: v163-171.
    • (1983) Biochim Biophys Acta , vol.733
    • Prado, A.1    Arrondo, J.L.2    Villena, A.3    Goni, F.M.4    Macarulla, J.M.5
  • 29
    • 0029731419 scopus 로고    scopus 로고
    • Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy
    • Reinstädler D, Fabian H, Backmann J, Naumann D (1996) Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy. Biochemistry 35: 15822-15830.
    • (1996) Biochemistry , vol.35 , pp. 15822-15830
    • Reinstädler, D.1    Fabian, H.2    Backmann, J.3    Naumann, D.4
  • 30
    • 0036787791 scopus 로고    scopus 로고
    • Effect of hydrophobic surfactant proteins SP-B and SP-C on phospholipid monolayers. Protein structure studied using 2D IR and beta correlation analysis
    • Shanmukh S, Howell P, Baatz JE, Dluhy RA (2002) Effect of hydrophobic surfactant proteins SP-B and SP-C on phospholipid monolayers. Protein structure studied using 2D IR and beta correlation analysis. Biophys J 83: 2126-2141.
    • (2002) Biophys J , vol.83 , pp. 2126-2141
    • Shanmukh, S.1    Howell, P.2    Baatz, J.E.3    Dluhy, R.A.4
  • 31
    • 0344404206 scopus 로고    scopus 로고
    • Reversible denaturation, self-aggregation, and membrane activity of Escherichia coli alpha-hemolysin, a protein stable in 6 M urea
    • Soloaga A, Ramirez JM, Goni FM (1998) Reversible denaturation, self-aggregation, and membrane activity of Escherichia coli alpha-hemolysin, a protein stable in 6 M urea. Biochemistry 37: 6387-6393.
    • (1998) Biochemistry , vol.37 , pp. 6387-6393
    • Soloaga, A.1    Ramirez, J.M.2    Goni, F.M.3
  • 32
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C (1968) Protein denaturation. Adv Protein Chem 23: 121-282.
    • (1968) Adv Protein Chem , vol.23 , pp. 121-282
    • Tanford, C.1
  • 33
    • 10744220126 scopus 로고    scopus 로고
    • Structural study of the C2 domains of the classical PKC isoenzymes using infrared spectroscopy and two-dimensional infrared correlation spectroscopy
    • Torrecillas A, Corbalan-Garcia S, Gomez-Fernandez JC (2003) Structural study of the C2 domains of the classical PKC isoenzymes using infrared spectroscopy and two-dimensional infrared correlation spectroscopy. Biochemistry 42: 11669-11681.
    • (2003) Biochemistry , vol.42 , pp. 11669-11681
    • Torrecillas, A.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 34
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
    • Toyoshima C, Nakasako M, Nomura H, Ogawa H (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405: 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 35
    • 0036788520 scopus 로고    scopus 로고
    • Calcium-dependent conformational rearrangements and protein stability in chicken annexin A5
    • Turnay J, Olmo N, Gasset M, Iloro I, Arrondo JL, Lizarbe MA (2002) Calcium-dependent conformational rearrangements and protein stability in chicken annexin A5. Biophys J 83: 2280-2291.
    • (2002) Biophys J , vol.83 , pp. 2280-2291
    • Turnay, J.1    Olmo, N.2    Gasset, M.3    Iloro, I.4    Arrondo, J.L.5    Lizarbe, M.A.6
  • 36
    • 0024576947 scopus 로고
    • Fourier transform infrared spectroscopic studies on the secondary structure of the Ca2+-ATPase of sarcoplasmic reticulum
    • Villalain J, Gomez-Fernandez JC, Jackson M, Chapman D (1989) Fourier transform infrared spectroscopic studies on the secondary structure of the Ca2+-ATPase of sarcoplasmic reticulum. Biochim Biophys Acta 978: 305-312.
    • (1989) Biochim Biophys Acta , vol.978 , pp. 305-312
    • Villalain, J.1    Gomez-Fernandez, J.C.2    Jackson, M.3    Chapman, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.