메뉴 건너뛰기




Volumn 266, Issue 2, 1997, Pages 223-230

Probing the conformational state of apomyoglobin by limited proteolysis

Author keywords

Apomyoglobin; Limited proteolysis; Mass spectrometry; Protein dynamics; Protein folding

Indexed keywords

CHYMOTRYPSIN; MYOGLOBIN; POLYPEPTIDE; PROTEINASE; SUBTILISIN; THERMOLYSIN; TRYPSIN;

EID: 0031581883     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0787     Document Type: Editorial
Times cited : (180)

References (52)
  • 1
    • 0027245421 scopus 로고
    • Three-state analysis of sperm whale apomyoglobin folding
    • Barrick D., Baldwin R. K. Three-state analysis of sperm whale apomyoglobin folding. Biochemistry. 34:1993;3790-3796.
    • (1993) Biochemistry , vol.34 , pp. 3790-3796
    • Barrick, D.1    Baldwin, R.K.2
  • 2
    • 0011201447 scopus 로고
    • Combination of protoporphirin IX with sperm whale myoglobin
    • Breslow E., Koehler R. Combination of protoporphirin IX with sperm whale myoglobin. J. Biol. Chem. 246:1965;2266-2268.
    • (1965) J. Biol. Chem , vol.246 , pp. 2266-2268
    • Breslow, E.1    Koehler, R.2
  • 3
    • 0027050472 scopus 로고
    • Structural analysis of wild-type and mutant yeast calmodulins by limited proteolysis and electrospray ionization mass spectrometry
    • Brockerhoff S. E., Edmonds C. G., Davis T. N. Structural analysis of wild-type and mutant yeast calmodulins by limited proteolysis and electrospray ionization mass spectrometry. Protein Sci. 1:1992;504-516.
    • (1992) Protein Sci. , vol.1 , pp. 504-516
    • Brockerhoff, S.E.1    Edmonds, C.G.2    Davis, T.N.3
  • 4
    • 0026731467 scopus 로고
    • Characterization of "native" apomyoglobin by molecular dynamics simulation
    • Brooks C. L. Characterization of "native" apomyoglobin by molecular dynamics simulation. J. Mol. Biol. 227:1992;375-380.
    • (1992) J. Mol. Biol. , vol.227 , pp. 375-380
    • Brooks, C.L.1
  • 5
    • 0025616115 scopus 로고
    • Characterization of hydrophobic cores in apomyoglobin: A proton NMR spectroscopy study
    • Cocco M. J., Lecomte J. T. J. Characterization of hydrophobic cores in apomyoglobin: a proton NMR spectroscopy study. Biochemistry. 29:1990;11067-11072.
    • (1990) Biochemistry , vol.29 , pp. 11067-11072
    • Cocco, M.J.1    Lecomte, J.T.J.2
  • 6
    • 0028299603 scopus 로고
    • The native state of apomyoglobin described by proton NMR spectroscopy: Interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS
    • Cocco M. J., Lecomte J. T. J. The native state of apomyoglobin described by proton NMR spectroscopy: interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS. Protein Sci. 3:1994;267-281.
    • (1994) Protein Sci. , vol.3 , pp. 267-281
    • Cocco, M.J.1    Lecomte, J.T.J.2
  • 7
    • 0026643349 scopus 로고
    • Structural comparison of apomyoglobin and metaquomyoglobin: PH titration of histidines by NMR spectroscopy
    • Cocco M. J., Kao Y. H., Phillips A. T., Lecomte J. T. J. Structural comparison of apomyoglobin and metaquomyoglobin: pH titration of histidines by NMR spectroscopy. Biochemistry. 31:1992;6481-6491.
    • (1992) Biochemistry , vol.31 , pp. 6481-6491
    • Cocco, M.J.1    Kao, Y.H.2    Phillips, A.T.3    Lecomte, J.T.J.4
  • 8
    • 0029004044 scopus 로고
    • Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry
    • Cohen S. L., Ferrè-D'Amarè A. R., Burley K. S., Chait B. T. Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry. Protein Sci. 4:1995;1088-1099.
    • (1995) Protein Sci. , vol.4 , pp. 1088-1099
    • Cohen, S.L.1    Ferrè-D'Amarè, A.R.2    Burley, K.S.3    Chait, B.T.4
  • 9
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • Eliezer D., Knight P. E. Is apomyoglobin a molten globule? Structural characterization by NMR. J. Mol. Biol. 263:1996;531-538.
    • (1996) J. Mol. Biol. , vol.263 , pp. 531-538
    • Eliezer, D.1    Knight, P.E.2
  • 10
    • 0025296867 scopus 로고
    • High-resolution study of the three-dimensional structure of horse heart metmyoglobin
    • Evans S. V., Brayer G. D. High-resolution study of the three-dimensional structure of horse heart metmyoglobin. J. Mol. Biol. 213:1990;885-897.
    • (1990) J. Mol. Biol. , vol.213 , pp. 885-897
    • Evans, S.V.1    Brayer, G.D.2
  • 11
    • 0002510219 scopus 로고
    • Fragmentation of polypeptides by chemical methods
    • Chichester: J. Wiley and Sons
    • Fontana A., Gross E. Fragmentation of polypeptides by chemical methods. Practical Protein Chemistry: A Handbook. 1986;J. Wiley and Sons, Chichester.
    • (1986) Practical Protein Chemistry: a Handbook
    • Fontana, A.1    Gross, E.2
  • 12
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana A., Fassina G., Vita C., Dalzoppo D., Zamai M., Zambonin M. Correlation between sites of limited proteolysis and segmental mobility in thermolysin. Biochemistry. 25:1986;1847-1851.
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 13
    • 0003831915 scopus 로고
    • Molecular aspects of proteolysis of globular proteins
    • W. van den Tweel, A. Harder, & M. Buitelear. Amsterdam: Elsevier Science Publ.
    • Fontana A., Polverino de Laureto P., De Filippis V. Molecular aspects of proteolysis of globular proteins. van den Tweel W., Harder A., Buitelear M. Protein Stability and Stabilization. 1993;Elsevier Science Publ. Amsterdam.
    • (1993) Protein Stability and Stabilization
    • Fontana, A.1    De Polverino Laureto, P.2    De Filippis, V.3
  • 15
    • 0025026407 scopus 로고
    • Phase diagram for acidic conformational states of apomyoglobin
    • Goto Y., Fink A. L. Phase diagram for acidic conformational states of apomyoglobin. J. Mol. Biol. 214:1990;803-805.
    • (1990) J. Mol. Biol. , vol.214 , pp. 803-805
    • Goto, Y.1    Fink, A.L.2
  • 16
    • 0028329347 scopus 로고
    • Thermodynamic puzzle of apomyoglobin unfolding
    • Griko Y. V., Privalov P. L. Thermodynamic puzzle of apomyoglobin unfolding. J. Mol. Biol. 235:1994;1318-1325.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1318-1325
    • Griko, Y.V.1    Privalov, P.L.2
  • 18
    • 0014429123 scopus 로고
    • Comparison of myoglobin from harbor seal, porpoise and sperm whale. I. Preparation and characterization
    • Hapner K. D., Bradshaw R. A., Hartzell C. R., Gurd F. R. N. Comparison of myoglobin from harbor seal, porpoise and sperm whale. I. Preparation and characterization. J. Biol. Chem. 243:1968;683-689.
    • (1968) J. Biol. Chem. , vol.243 , pp. 683-689
    • Hapner, K.D.1    Bradshaw, R.A.2    Hartzell, C.R.3    Gurd, F.R.N.4
  • 19
    • 0000707259 scopus 로고
    • Reversible conformational changes of myoglobin and apomyoglobin
    • Harrison S. C., Blout E. R. Reversible conformational changes of myoglobin and apomyoglobin. J. Biol. Chem. 240:1965;299-303.
    • (1965) J. Biol. Chem. , vol.240 , pp. 299-303
    • Harrison, S.C.1    Blout, E.R.2
  • 20
    • 0028019116 scopus 로고
    • Helicity, circular dichroism and molecular dynamics of proteins
    • Hirst J. D., Brooks C. L. Helicity, circular dichroism and molecular dynamics of proteins. J. Mol. Biol. 243:1994;173-178.
    • (1994) J. Mol. Biol. , vol.243 , pp. 173-178
    • Hirst, J.D.1    Brooks, C.L.2
  • 21
    • 0025912338 scopus 로고
    • Molecular recognition: Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors
    • Hubbard S. J., Campbell S. F., Thornton J. M. Molecular recognition: Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors. J. Mol. Biol. 220:1991;507-530.
    • (1991) J. Mol. Biol. , vol.220 , pp. 507-530
    • Hubbard, S.J.1    Campbell, S.F.2    Thornton, J.M.3
  • 22
    • 0028336661 scopus 로고
    • Modeling studies of the change in conformation required for cleavage of limited proteolytic sites
    • Hubbard S. J., Eisenmenger F., Thornton J. M. Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Sci. 3:1994;757-768.
    • (1994) Protein Sci. , vol.3 , pp. 757-768
    • Hubbard, S.J.1    Eisenmenger, F.2    Thornton, J.M.3
  • 23
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson F. M., Wright P. E., Baldwin R. L. Structural characterization of a partly folded apomyoglobin intermediate. Science. 249:1990;1544-1548.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 24
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings P. A., Wright P. E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science. 262:1993;892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 25
    • 0029032691 scopus 로고
    • Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka M., Nishii I., Fujisawa T., Ueki T., Tokunaga F., Goto Y. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249:1995;215-228.
    • (1995) J. Mol. Biol. , vol.249 , pp. 215-228
    • Kataoka, M.1    Nishii, I.2    Fujisawa, T.3    Ueki, T.4    Tokunaga, F.5    Goto, Y.6
  • 26
    • 0002916242 scopus 로고
    • Enzymic cleavage of proteins
    • M. Elzinga. Clifton: Humana Press
    • Keil B. Enzymic cleavage of proteins. Elzinga M. Methods in Protein Sequence Analysis. 1982;Humana Press, Clifton.
    • (1982) Methods in Protein Sequence Analysis
    • Keil, B.1
  • 27
    • 0024341206 scopus 로고
    • Gas-phase sequencing after electroblotting on polyvinylidene difluoride membranes assigns correct molecular weights to myoglobin molecular weight markers
    • Kratzin H. D., Wiltfang J., Karas M., Neuhoff V., Hilschmann N. Gas-phase sequencing after electroblotting on polyvinylidene difluoride membranes assigns correct molecular weights to myoglobin molecular weight markers. Anal. Biochem. 183:1989;1-8.
    • (1989) Anal. Biochem. , vol.183 , pp. 1-8
    • Kratzin, H.D.1    Wiltfang, J.2    Karas, M.3    Neuhoff, V.4    Hilschmann, N.5
  • 28
    • 0023042853 scopus 로고
    • X-ray structure and refinement of carbon-monoxy (Fe-II)-myoglobin at 1.5 Å resolution
    • Kuriyan J., Wilz S., Karplus M., Petsko G. A. X-ray structure and refinement of carbon-monoxy (Fe-II)-myoglobin at 1.5 Å resolution. J. Mol. Biol. 245:1986;133-154.
    • (1986) J. Mol. Biol. , vol.245 , pp. 133-154
    • Kuriyan, J.1    Wilz, S.2    Karplus, M.3    Petsko, G.A.4
  • 29
    • 0030056766 scopus 로고    scopus 로고
    • The native state of apomyoglobin described by proton NMR spectroscopy: The A-B-G-H interface of wild-type sperm whale apomyoglobin
    • Lecomte J. T. J., Kao Y.-H., Cocco M. J. The native state of apomyoglobin described by proton NMR spectroscopy: The A-B-G-H interface of wild-type sperm whale apomyoglobin. Proteins: Struct. Funct. Genet. 25:1996;267-285.
    • (1996) Proteins: Struct. Funct. Genet. , vol.25 , pp. 267-285
    • Lecomte, J.T.J.1    Kao, Y.-H.2    Cocco, M.J.3
  • 31
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh S. N., Kay M. S., Baldwin R. L. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Natl. Acad. Sci. USA. 92:1995;5446-5450.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3
  • 32
    • 0018146009 scopus 로고
    • Is protein turnover thermodynamically controlled?
    • McLendon G., Radany E. Is protein turnover thermodynamically controlled? J. Biol. Chem. 253:1978;6335-6337.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6335-6337
    • McLendon, G.1    Radany, E.2
  • 34
    • 0028959010 scopus 로고
    • Ligand-induced conformational changes of thymidylate synthase detected by limited proteolysis
    • Mohsen A. A., Aull J. L., Payne D. M., Daron H. M. Ligand-induced conformational changes of thymidylate synthase detected by limited proteolysis. Biochemistry. 34:1995;1669-1677.
    • (1995) Biochemistry , vol.34 , pp. 1669-1677
    • Mohsen, A.A.1    Aull, J.L.2    Payne, D.M.3    Daron, H.M.4
  • 35
    • 0028243107 scopus 로고
    • Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
    • Nishii I., Kataoka M., Tokunaga F., Goto Y. Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry. 33:1994;4903-4909.
    • (1994) Biochemistry , vol.33 , pp. 4903-4909
    • Nishii, I.1    Kataoka, M.2    Tokunaga, F.3    Goto, Y.4
  • 36
    • 0029040449 scopus 로고
    • Thermodynamic stability of the molten globule states of apomyoglobin
    • Nishii I., Kataoka M., Goto Y. Thermodynamic stability of the molten globule states of apomyoglobin. J. Mol. Biol. 250:1995;223-238.
    • (1995) J. Mol. Biol. , vol.250 , pp. 223-238
    • Nishii, I.1    Kataoka, M.2    Goto, Y.3
  • 37
    • 0023140225 scopus 로고
    • Correlation among sites of limited proteolysis, enzyme accessibility and segmental mobility
    • Novotny J., Bruccoleri R. E. Correlation among sites of limited proteolysis, enzyme accessibility and segmental mobility. FEBS Letters. 211:1987;185-189.
    • (1987) FEBS Letters , vol.211 , pp. 185-189
    • Novotny, J.1    Bruccoleri, R.E.2
  • 38
    • 0029873754 scopus 로고    scopus 로고
    • The domain organization of streptokinase: Nuclear magnetic resonance, circular dichroism and functional characterization of proteolytic fragments
    • Parrado J., Conejero-Lara F., Smith R. A. G., Marshall J. M., Ponting C. P., Dobson C. M. The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism and functional characterization of proteolytic fragments. Protein Sci. 5:1996;693-704.
    • (1996) Protein Sci. , vol.5 , pp. 693-704
    • Parrado, J.1    Conejero-Lara, F.2    Smith, R.A.G.3    Marshall, J.M.4    Ponting, C.P.5    Dobson, C.M.6
  • 41
    • 0029012839 scopus 로고
    • Limited proteolysis of lysozyme in trifluoroethanol: Isolation and characterization of a partially active enzyme derivative
    • Polverino de Laureto P., De Filippis V., Scaramella E., Zambonin M., Fontana A. Limited proteolysis of lysozyme in trifluoroethanol: Isolation and characterization of a partially active enzyme derivative. Eur. J. Biochem. 230:1995b;779-787.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 779-787
    • De Polverino Laureto, P.1    De Filippis, V.2    Scaramella, E.3    Zambonin, M.4    Fontana, A.5
  • 43
    • 0000352442 scopus 로고
    • Proteinases as probes of conformation of soluble proteins
    • R.J. Beynon, & J.S. Bond. Oxford: IRL Press
    • Price N. C., Johnson C. M. Proteinases as probes of conformation of soluble proteins. Beynon R. J., Bond J. S. Proteolytic Enzymes: A Practical Approach. 1990;IRL Press, Oxford.
    • (1990) Proteolytic Enzymes: a Practical Approach
    • Price, N.C.1    Johnson, C.M.2
  • 44
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:1987;368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 45
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:1967;157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 46
    • 0028862855 scopus 로고
    • Analysis of the structural core of the human estrogen receptor ligand binding domain by selective proteolysis/mass spectrometric analysis
    • Seielstad D. A., Carlson K. E., Kushner P. J., Greene G. L., Katzenellenbogen J. A. Analysis of the structural core of the human estrogen receptor ligand binding domain by selective proteolysis/mass spectrometric analysis. Biochemistry. 34:1995;12605-12615.
    • (1995) Biochemistry , vol.34 , pp. 12605-12615
    • Seielstad, D.A.1    Carlson, K.E.2    Kushner, P.J.3    Greene, G.L.4    Katzenellenbogen, J.A.5
  • 48
    • 0013800421 scopus 로고
    • The interaction of a naphtalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Stryer L. The interaction of a naphtalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13:1965;482-495.
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 49
    • 0017364269 scopus 로고
    • Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of sperm whale met-myoglobin
    • Takano T. Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of sperm whale met-myoglobin. J. Mol. Biol. 110:1977;537-568.
    • (1977) J. Mol. Biol. , vol.110 , pp. 537-568
    • Takano, T.1
  • 50
    • 0027316216 scopus 로고
    • Molecular dynamics simulations of the unfolding of apomyoglobin in water
    • Tirado-Rives J., Jorgensen W. L. Molecular dynamics simulations of the unfolding of apomyoglobin in water. Biochemistry. 32:1993;4175-4184.
    • (1993) Biochemistry , vol.32 , pp. 4175-4184
    • Tirado-Rives, J.1    Jorgensen, W.L.2
  • 51
    • 0028361968 scopus 로고
    • Structural origins of pH and ionic strength effects on protein stability: Acid denaturation of sperm whale apomyoglobin
    • Yang A.-S., Honig B. Structural origins of pH and ionic strength effects on protein stability: Acid denaturation of sperm whale apomyoglobin. J. Mol. Biol. 237:1994;602-614.
    • (1994) J. Mol. Biol. , vol.237 , pp. 602-614
    • Yang, A.-S.1    Honig, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.