메뉴 건너뛰기




Volumn 1814, Issue 8, 2011, Pages 934-941

Protein dynamics and pressure: What can high pressure tell us about protein structural flexibility?

Author keywords

Azurin; High pressure; Protein cavities; Protein dynamics; Protein structure; Tryptophan phosphorescence

Indexed keywords

AZURIN; POLYPEPTIDE;

EID: 79958782065     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.09.017     Document Type: Review
Times cited : (24)

References (100)
  • 1
    • 0033230717 scopus 로고    scopus 로고
    • Pressure-regulated metabolism in microorganisms
    • DOI 10.1016/S0966-842X(99)01608-X, PII S0966842X9901608X
    • F. Abe, C. Kato, K. Horikoshi, Pressure-regulated metabolism in microorganisms, Trends Microbiol. 7 (1999) 447-453. (Pubitemid 29528232)
    • (1999) Trends in Microbiology , vol.7 , Issue.11 , pp. 447-453
    • Abe, F.1    Kato, C.2    Horikoshi, K.3
  • 4
    • 68349117194 scopus 로고    scopus 로고
    • Effects of hydrostatic pressure on the stability and thermostability of poliovirus: A new method for vaccine preservation
    • E. Ferreira, Y.S. Mendes, J.L. Silva, R. Galler, A.C. Oliveira, M.S. Freire, L.P. Gaspar, Effects of hydrostatic pressure on the stability and thermostability of poliovirus: a new method for vaccine preservation, Vaccine 27 (2009) 5332-5337.
    • (2009) Vaccine , vol.27 , pp. 5332-5337
    • Ferreira, E.1    Mendes, Y.S.2    Silva, J.L.3    Galler, R.4    Oliveira, A.C.5    Freire, M.S.6    Gaspar, L.P.7
  • 5
    • 0019363271 scopus 로고
    • Enzymes under extremes of physical conditions
    • R. Jaenicke, Enzymes under extremes of physical conditions, Annu. Rev. Biophys. Bioeng. 10 (1981) 1-67.
    • (1981) Annu. Rev. Biophys. Bioeng. , vol.10 , pp. 1-67
    • Jaenicke, R.1
  • 9
    • 34249723738 scopus 로고    scopus 로고
    • High-pressure biotechnology in medicine and pharmaceutical science
    • P. Masson, C. Tonello, C. Balny, High-pressure biotechnology in medicine and pharmaceutical science, J. Biomed. Biotechnol. 1 (2001) 85-88.
    • (2001) J. Biomed. Biotechnol. , vol.1 , pp. 85-88
    • Masson, P.1    Tonello, C.2    Balny, C.3
  • 11
    • 77949558315 scopus 로고    scopus 로고
    • A brief overview of the effect of high pressures on the vibrational spectra of biomaterials
    • A. Tiwari, I.S. Butler, J.A. Kozinski, A brief overview of the effect of high pressures on the vibrational spectra of biomaterials, Appl. Spectrosc. Rev. 44 (2009) 552-567.
    • (2009) Appl. Spectrosc. Rev. , vol.44 , pp. 552-567
    • Tiwari, A.1    Butler, I.S.2    Kozinski, J.A.3
  • 12
    • 70350572357 scopus 로고    scopus 로고
    • Compressibility anddensity of select liquid and solid foods under pressures up to 700 MPa
    • S.Min, S.K. Sastry,W.M.Balasubramaniam, Compressibility anddensity of select liquid and solid foods under pressures up to 700 MPa, J. Food Eng. 96 (2010) 568-574.
    • (2010) J. Food Eng. , vol.96 , pp. 568-574
    • Min, S.1    Sastry, S.K.2    Balasubramaniam, W.M.3
  • 13
    • 33645973697 scopus 로고    scopus 로고
    • What lies in the future of high-pressure bioscience?
    • C. Balny, What lies in the future of high-pressure bioscience? Biochim. Biophys. Acta 1764 (2006) 632-639.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 632-639
    • Balny, C.1
  • 14
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • G. Weber, H.G. Drickamer, The effect of high pressure upon proteins and other biomolecules, Q. Rev. Biophys. 16 (1983) 89-112.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2
  • 15
    • 20144369761 scopus 로고    scopus 로고
    • Stability of proteins: Temperature, pressure and the role of the solvent
    • DOI 10.1016/j.bbapap.2005.03.002, PII S1570963905000890, Solvent Effects
    • C. Scharnagl, M. Reif, J. Friedrich, Stability of proteins: temperature, pressure and the role of the solvent, Biochim. Et Biophys. Acta Proteins Proteomics 1749 (2005) 187-213. (Pubitemid 40775865)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1749 , Issue.2 , pp. 187-213
    • Scharnagl, C.1    Reif, M.2    Friedrich, J.3
  • 16
    • 61749085446 scopus 로고    scopus 로고
    • Protein cold denaturation as seen from the solvent
    • M. Davidovic, C. Mattea, J. Qvist, B. Halle, Protein cold denaturation as seen from the solvent, J. Am. Chem. Soc. 131 (2009) 1025-1036.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1025-1036
    • Davidovic, M.1    Mattea, C.2    Qvist, J.3    Halle, B.4
  • 18
    • 34547751872 scopus 로고    scopus 로고
    • Protein disaggregation and refolding using high hydrostatic pressure
    • DOI 10.1002/jctb.1707
    • D.J. Phelps, L.K. Hesterberg, Protein disaggregation and refolding using high hydrostatic pressure, J. Chem. Technol. Biotechnol. 82 (2007) 610-613. (Pubitemid 47224519)
    • (2007) Journal of Chemical Technology and Biotechnology , vol.82 , Issue.7 , pp. 610-613
    • Phelps, D.J.1    Hesterberg, L.K.2
  • 20
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • A. Cooper, Thermodynamic fluctuations in protein molecules, Proc. Natl Acad. Sci. USA 73 (1976) 2740-2741.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 21
    • 0033609806 scopus 로고    scopus 로고
    • Pressure/temperature effects on protein flexibility from acrylamide quenching of protein phosphorescence
    • P. Cioni, G.B. Strambini, Pressure/temperature effects on protein flexibility from acrylamide quenching of protein phosphorescence, J. Mol. Biol. 291 (1999) 955-964.
    • (1999) J. Mol. Biol. , vol.291 , pp. 955-964
    • Cioni, P.1    Strambini, G.B.2
  • 22
    • 0027934772 scopus 로고
    • Pressure effects on protein flexibility monomeric proteins
    • P. Cioni, G.B. Strambini, Pressure effects on protein flexibility monomeric proteins, J. Mol. Biol. 242 (1994) 291-301.
    • (1994) J. Mol. Biol. , vol.242 , pp. 291-301
    • Cioni, P.1    Strambini, G.B.2
  • 26
    • 33847308554 scopus 로고    scopus 로고
    • Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography
    • M.D. Collins, M.L. Quillin, G. Hummer, B.W. Matthews, S.M. Gruner, Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography, J. Mol. Biol. 367 (2007) 752-763.
    • (2007) J. Mol. Biol. , vol.367 , pp. 752-763
    • Collins, M.D.1    Quillin, M.L.2    Hummer, G.3    Matthews, B.W.4    Gruner, S.M.5
  • 27
    • 33646900712 scopus 로고    scopus 로고
    • Probing conformational fluctuation of proteins by pressure perturbation
    • K. Akasaka, Probing conformational fluctuation of proteins by pressure perturbation, Chem. Rev. 106 (2006) 1814-1835.
    • (2006) Chem. Rev. , vol.106 , pp. 1814-1835
    • Akasaka, K.1
  • 28
    • 33748176879 scopus 로고    scopus 로고
    • Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy
    • N. Kachel, W. Kremer, R. Zahn, H.R. Kalbitzer, Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy, BMC Struct. Biol. 6 (2006) 16.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 16
    • Kachel, N.1    Kremer, W.2    Zahn, R.3    Kalbitzer, H.R.4
  • 29
    • 33645981275 scopus 로고    scopus 로고
    • Conformational fluctuations of proteins revealed by variable pressure NMR
    • H. Li, K. Akasaka, Conformational fluctuations of proteins revealed by variable pressure NMR, Biochim. Biophys. Acta 1764 (2006) 331-345.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 331-345
    • Li, H.1    Akasaka, K.2
  • 30
    • 0042511922 scopus 로고    scopus 로고
    • The solution structure of bovine pancreatic trypsin inhibitor at high pressure
    • DOI 10.1110/ps.0242103
    • M.P. Williamson, K. Akasaka, M. Refaee, The solution structure of bovine pancreatic trypsin inhibitor at high pressure, Protein Sci. 12 (2003) 1971-1979. (Pubitemid 37022819)
    • (2003) Protein Science , vol.12 , Issue.9 , pp. 1971-1979
    • Williamson, M.P.1    Akasaka, K.2    Refaee, M.3
  • 31
    • 0023644307 scopus 로고
    • Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres
    • C.E. Kundrot, F.M. Richards, Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres, J. Mol. Biol. 193 (1987) 157-170.
    • (1987) J. Mol. Biol. , vol.193 , pp. 157-170
    • Kundrot, C.E.1    Richards, F.M.2
  • 32
    • 70349606921 scopus 로고    scopus 로고
    • Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations
    • D.J. Wilton, R. Kitahara, K. Akasaka, M.J. Pandya, M.P. Williamson, Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations, Biophys. J. 97 (2009) 1482-1490.
    • (2009) Biophys. J. , vol.97 , pp. 1482-1490
    • Wilton, D.J.1    Kitahara, R.2    Akasaka, K.3    Pandya, M.J.4    Williamson, M.P.5
  • 33
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar
    • R. Kitahara, S. Yokoyama, K. Akasaka, NMR snapshots of a fluctuating protein structure: ubiquitin at 30 bar-3 kbar, J. Mol. Biol. 347 (2005) 277-285.
    • (2005) J. Mol. Biol. , vol.347 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 34
    • 77649105245 scopus 로고    scopus 로고
    • Dynamic correlation between pressure-induced protein structural transition and water penetration
    • T. Imai, Y. Sugita, Dynamic correlation between pressure-induced protein structural transition and water penetration. J Phys Chem B, 114:2281-2286
    • J Phys Chem B , vol.114 , pp. 2281-2286
    • Imai, T.1    Sugita, Y.2
  • 35
    • 0344406172 scopus 로고    scopus 로고
    • Pressure-dependent changes in the solution structure of hen egg-white lysozyme
    • M. Refaee, T. Tezuka, K. Akasaka, M.P. Williamson, Pressure-dependent changes in the solution structure of hen egg-white lysozyme, J. Mol. Biol. 327 (2003) 857-865.
    • (2003) J. Mol. Biol. , vol.327 , pp. 857-865
    • Refaee, M.1    Tezuka, T.2    Akasaka, K.3    Williamson, M.P.4
  • 37
    • 0032347515 scopus 로고    scopus 로고
    • Compressibility and volume changes of lysozyme due to inhibitor binding
    • K. Gekko, K. Yamagami, Compressibility and volume changes of lysozyme due to inhibitor binding, Chem. Lett. (1998) 839-840.
    • (1998) Chem. Lett. , pp. 839-840
    • Gekko, K.1    Yamagami, K.2
  • 39
    • 17844397457 scopus 로고    scopus 로고
    • The first crystal structure of a macromolecular assembly under high pressure: CpMV at 330 MPa
    • DOI 10.1529/biophysj.104.058636
    • E. Girard, R. Kahn, M. Mezouar, A.C. Dhaussy, T.W. Lin, J.E. Johnson, R. Fourme, The first crystal structure of a macromolecular assembly under high pressure: CpMV at 330 MPa, Biophys. J. 88 (2005) 3562-3571. (Pubitemid 40586604)
    • (2005) Biophysical Journal , vol.88 , Issue.5 , pp. 3562-3571
    • Girard, E.1    Kahn, R.2    Mezouar, M.3    Dhaussy, A.-C.4    Lin, T.5    Johnson, J.E.6    Fourme, R.7
  • 40
    • 0036774089 scopus 로고    scopus 로고
    • Opening the high-pressure domain beyond 2 kbar to protein and virus crystallography: Technical advance
    • DOI 10.1016/S0969-2126(02)00850-X, PII S096921260200850X
    • R. Fourme, I. Ascone, R. Kahn, M. Mezouar, P. Bouvier, E. Girard, T.W. Lin, J.E. Johnson, Opening the high-pressure domain beyond 2 kbar to protein and virus crystallography-technical advance, Structure 10 (2002) 1409-1414. (Pubitemid 35232386)
    • (2002) Structure , vol.10 , Issue.10 , pp. 1409-1414
    • Fourme, R.1    Ascone, I.2    Kahn, R.3    Mezouar, M.4    Bouvier, P.5    Girard, E.6    Lin, T.7    Johnson, J.E.8
  • 41
    • 67650319011 scopus 로고    scopus 로고
    • Advances in high-pressure biophysics: Status and prospects of macromolecular crystallography
    • R. Fourme, E. Girard, R. Kahn, A.C. Dhaussy, I. Ascone, Advances in high-pressure biophysics: status and prospects of macromolecular crystallography, Annu. Rev. Biophys. 38 (2009) 153-171.
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 153-171
    • Fourme, R.1    Girard, E.2    Kahn, R.3    Dhaussy, A.C.4    Ascone, I.5
  • 42
    • 33646490977 scopus 로고    scopus 로고
    • High pressure macromolecular crystallography: The 140-MPa crystal structure at 2.3 A resolution of urate oxidase, a 135-kDa tetrameric assembly
    • N. Colloc'h, E. Girard, A.C. Dhaussy, R. Kahn, I. Ascone, M. Mezouar, R. Fourme, High pressure macromolecular crystallography: the 140-MPa crystal structure at 2.3 A resolution of urate oxidase, a 135-kDa tetrameric assembly, Biochim. Biophys. Acta 1764 (2006) 391-397.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 391-397
    • Colloc'H, N.1    Girard, E.2    Dhaussy, A.C.3    Kahn, R.4    Ascone, I.5    Mezouar, M.6    Fourme, R.7
  • 43
    • 0036154017 scopus 로고    scopus 로고
    • Probing substates in sperm whale myoglobin using high-pressure crystallography
    • DOI 10.1016/S0969-2126(01)00699-2, PII S0969212601006992
    • P. Urayama, G.N. Phillips Jr., S.M. Gruner, Probing substates in sperm whale myoglobin using high-pressure crystallography, Structure 10 (2002) 51-60. (Pubitemid 34112610)
    • (2002) Structure , vol.10 , Issue.1 , pp. 51-60
    • Urayama, P.1    Phillips Jr., G.N.2    Gruner, S.M.3
  • 45
    • 77952511233 scopus 로고    scopus 로고
    • Flexibility of the Cu, Zn superoxide dismutase structure investigated at 0.57 GPa
    • I. Ascone, C. Savino, R. Kahn, R. Fourme, Flexibility of the Cu, Zn superoxide dismutase structure investigated at 0.57 GPa, Acta Crystallogr. D Biol. Crystallogr. 66 (2010) 654-663.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 654-663
    • Ascone, I.1    Savino, C.2    Kahn, R.3    Fourme, R.4
  • 49
    • 70350028297 scopus 로고    scopus 로고
    • Coupling of pressure-induced structural shifts to spectral changes in a yellow fluorescent protein
    • B. Barstow, N. Ando, C.U. Kim, S.M. Gruner, Coupling of pressure-induced structural shifts to spectral changes in a yellow fluorescent protein, Biophys. J. 97 (2009) 1719-1727.
    • (2009) Biophys. J. , vol.97 , pp. 1719-1727
    • Barstow, B.1    Ando, N.2    Kim, C.U.3    Gruner, S.M.4
  • 50
    • 0035800773 scopus 로고    scopus 로고
    • Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications
    • O. Griesbeck, G.S. Baird, R.E. Campbell, D.A. Zacharias, R.Y. Tsien, Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications, J. Biol. Chem. 276 (2001) 29188-29194.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29188-29194
    • Griesbeck, O.1    Baird, G.S.2    Campbell, R.E.3    Zacharias, D.A.4    Tsien, R.Y.5
  • 51
    • 0032532156 scopus 로고    scopus 로고
    • Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein
    • R.M. Wachter, M.A. Elsliger, K. Kallio, G.T. Hanson, S.J. Remington, Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein, Structure 6 (1998) 1267-1277. (Pubitemid 28485959)
    • (1998) Structure , vol.6 , Issue.10 , pp. 1267-1277
    • Wachter, R.M.1    Elsliger, M.-A.2    Kallio, K.3    Hanson, G.T.4    Remington, S.J.5
  • 52
    • 51649104603 scopus 로고    scopus 로고
    • Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift
    • B. Barstow, N. Ando, C.U. Kim, S.M. Gruner, Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift, Proc. Natl Acad. Sci. USA 105 (2008) 13362-13366.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 13362-13366
    • Barstow, B.1    Ando, N.2    Kim, C.U.3    Gruner, S.M.4
  • 53
    • 10044219858 scopus 로고    scopus 로고
    • Room temperature spectrally resolved single-molecule spectroscopy reveals new spectral forms and photophysical versatility of Aequorea green fluorescent protein variants
    • DOI 10.1529/biophysj.104.049452
    • C. Blum, A.J. Meixner, V. Subramaniam, Room temperature spectrally resolved single-molecule spectroscopy reveals new spectral forms and photophysical versatility of aequorea green fluorescent protein variants, Biophys. J. 87 (2004) 4172-4179. (Pubitemid 39602921)
    • (2004) Biophysical Journal , vol.87 , Issue.6 , pp. 4172-4179
    • Blum, C.1    Meixner, A.J.2    Subramaniam, V.3
  • 54
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • DOI 10.1038/nature06522, PII NATURE06522
    • K. Henzler-Wildman, D. Kern, Dynamic personalities of proteins, Nature 450 (2007) 964-972. (Pubitemid 350273626)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 55
    • 0000591693 scopus 로고
    • Room temperature phosphorescence and the dynamic aspects of protein structure
    • M.L. Saviotti, W.C. Galley, Room temperature phosphorescence and the dynamic aspects of protein structure, Proc. Natl Acad. Sci. USA 71 (1974) 4154-4158.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 4154-4158
    • Saviotti, M.L.1    Galley, W.C.2
  • 57
    • 0024508592 scopus 로고
    • Relationship between the conformation of glutamate dehydrogenase, the state of association of its subunit, and catalytic function
    • G.B. Strambini, P. Cioni, A. Puntoni, Relationship between the conformation of glutamate dehydrogenase, the state of association of its subunit, and catalytic function, Biochemistry 28 (1989) 3808-3814.
    • (1989) Biochemistry , vol.28 , pp. 3808-3814
    • Strambini, G.B.1    Cioni, P.2    Puntoni, A.3
  • 58
    • 0036114440 scopus 로고    scopus 로고
    • Effect of heavy water on protein flexibility
    • P. Cioni, G.B. Strambini, Effect of heavy water on protein flexibility, Biophys. J. 82 (2002) 3246-3253. (Pubitemid 34547668)
    • (2002) Biophysical Journal , vol.82 , Issue.6 , pp. 3246-3253
    • Cioni, P.1    Strambini, G.B.2
  • 59
    • 0037171150 scopus 로고    scopus 로고
    • Tryptophan phosphorescence and pressure effects on protein structure
    • P. Cioni, G.B. Strambini, Tryptophan phosphorescence and pressure effects on protein structure, Biochim. Biophys. Acta 1595 (2002) 116-130.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 116-130
    • Cioni, P.1    Strambini, G.B.2
  • 60
    • 46449085055 scopus 로고    scopus 로고
    • Effects of sugars and polyols on the stability of azurin in ice
    • G.B. Strambini, E. Balestreri, A. Galli, M. Gonnelli, Effects of sugars and polyols on the stability of azurin in ice, J. Phys. Chem. B 112 (2008) 4372-4380.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 4372-4380
    • Strambini, G.B.1    Balestreri, E.2    Galli, A.3    Gonnelli, M.4
  • 61
    • 59349115572 scopus 로고    scopus 로고
    • No effect of covalently linked poly(ethylene glycol) chains on protein internal dynamics
    • M. Gonnelli, G.B. Strambini, No effect of covalently linked poly(ethylene glycol) chains on protein internal dynamics, Biochim. Biophys. Acta 1794 (2009) 569-576.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 569-576
    • Gonnelli, M.1    Strambini, G.B.2
  • 62
    • 0017078830 scopus 로고
    • Kinetics of triplet-triplet energy transfer and intramolecular distances in enzyme-inhibitor complexes
    • W.C. Galley, G.B. Strambini, Kinetics of triplet-triplet energy transfer and intramolecular distances in enzyme-inhibitor complexes, Nature 261 (1976) 521-522.
    • (1976) Nature , vol.261 , pp. 521-522
    • Galley, W.C.1    Strambini, G.B.2
  • 63
    • 0000145156 scopus 로고
    • Tryptophan phosphorescence in fluid solution
    • G.B. Strambini, M. Gonnelli, Tryptophan phosphorescence in fluid solution, J. Am. Chem. Soc. 117 (1995) 7646-7651.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7646-7651
    • Strambini, G.B.1    Gonnelli, M.2
  • 64
    • 0028866475 scopus 로고
    • Phosphorescence lifetime of tryptophan in proteins
    • M. Gonnelli, G.B. Strambini, Phosphorescence lifetime of tryptophan in proteins, Biochemistry 34 (1995) 13847-13857.
    • (1995) Biochemistry , vol.34 , pp. 13847-13857
    • Gonnelli, M.1    Strambini, G.B.2
  • 65
    • 0002481190 scopus 로고
    • Tryptophan phosphorescence as monitor of protein flexibility
    • G.B. Strambini, Tryptophan phosphorescence as monitor of protein flexibility, J. Mol. Liq. 42 (1989) 155-165.
    • (1989) J. Mol. Liq. , vol.42 , pp. 155-165
    • Strambini, G.B.1
  • 66
    • 0021452281 scopus 로고
    • Intrinsic phosphorescence from proteins in the solid state
    • G.B. Strambini, E. Gabellieri, Intrinsic phosphorescence from proteins in the solid state, Photochem. Photobiol. 39 (1984) 725-729.
    • (1984) Photochem. Photobiol. , vol.39 , pp. 725-729
    • Strambini, G.B.1    Gabellieri, E.2
  • 67
    • 0027254999 scopus 로고
    • Glycerol effects on protein flexibility: A tryptophan phosphorescence study
    • M. Gonnelli, G.B. Strambini, Glycerol effects on protein flexibility: a tryptophan phosphorescence study, Biophys. J. 65 (1993) 131-137. (Pubitemid 23206046)
    • (1993) Biophysical Journal , vol.65 , Issue.1 , pp. 131-137
    • Gonnelli, M.1    Strambini, G.B.2
  • 68
    • 0024408792 scopus 로고
    • Tryptophan phosphorescence as a monitor of the structural role of metal ions in alkaline phosphatase
    • P. Cioni, L. Piras, G.B. Strambini, Tryptophan phosphorescence as a monitor of the structural role of metal ions in alkaline phosphatase, Eur. J. Biochem. 185 (1989) 573-579.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 573-579
    • Cioni, P.1    Piras, L.2    Strambini, G.B.3
  • 69
    • 0024364915 scopus 로고
    • Dynamical structure of glutamate dehydrogenase as monitored by tryptophan phosphorescence. Signal transmission following binding of allosteric effectors
    • DOI 10.1016/0022-2836(89)90453-1
    • P. Cioni, G.B. Strambini, Dynamical structure of glutamate dehydrogenase as monitored by tryptophan phosphorescence. Signal transmission following binding of allosteric effectors, J. Mol. Biol. 207 (1989) 237-247. (Pubitemid 19141254)
    • (1989) Journal of Molecular Biology , vol.207 , Issue.1 , pp. 237-247
    • Cioni, P.1    Strambini, G.B.2
  • 70
    • 0035041252 scopus 로고    scopus 로고
    • Structural perturbations of azurin deposited on solid matrices as revealed by trp phosphorescence
    • E. Gabellieri, G.B. Strambini, Structural perturbations of azurin deposited on solid matrices as revealed by trp phosphorescence, Biophys. J. 80 (2001) 2431-2438. (Pubitemid 32402005)
    • (2001) Biophysical Journal , vol.80 , Issue.5 , pp. 2431-2438
    • Gabellieri, E.1    Strambini, G.B.2
  • 71
    • 22244455728 scopus 로고    scopus 로고
    • Effects of sucrose on the internal dynamics of azurin
    • DOI 10.1529/biophysj.105.060517
    • P. Cioni, E. Bramanti, G.B. Strambini, Effects of sucrose on the internal dynamics of azurin, Biophys. J. 88 (2005) 4213-4222. (Pubitemid 40991132)
    • (2005) Biophysical Journal , vol.88 , Issue.6 , pp. 4213-4222
    • Cioni, P.1    Bramanti, E.2    Strambini, G.B.3
  • 72
    • 0015895751 scopus 로고
    • Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale
    • J.R. Lakowicz, G. Weber, Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale, Biochemistry 12 (1973) 4171-4179.
    • (1973) Biochemistry , vol.12 , pp. 4171-4179
    • Lakowicz, J.R.1    Weber, G.2
  • 73
    • 0023378095 scopus 로고
    • Quenching of alkaline phosphatase phosphorescence by O2 and NO. Evidence for inflexible regions of protein structure
    • G.B. Strambini, Quenching of alkaline phosphatase phosphorescence by O2 and NO. Evidence for inflexible regions of protein structure, Biophys J 52 (1987) 23-28.
    • (1987) Biophys J , vol.52 , pp. 23-28
    • Strambini, G.B.1
  • 74
    • 0032544957 scopus 로고    scopus 로고
    • Acrylamide quenching of protein phosphorescence as a monitor of structural fluctuations in the globular fold
    • DOI 10.1021/ja9820543
    • P. Cioni, G.B. Strambini, Acrylamide quenching of protein phosphorescence as a monitor of structural fluctuations in the globular fold, J. Am. Chem. Soc. 120 (1998) 11749-11757. (Pubitemid 28543587)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.45 , pp. 11749-11757
    • Cioni, P.1    Strambini, G.B.2
  • 75
    • 79958803889 scopus 로고
    • Plenum Publishing Corporation, New York
    • M.R. Eftink, Principles, Plenum Publishing Corporation, New York, 1991.
    • (1991) Principles
    • Eftink, M.R.1
  • 76
    • 0033568619 scopus 로고    scopus 로고
    • Pressure-temperature effects on oxygen quenching of protein phosphorescence
    • G.B. Strambini, P. Cioni, Pressure-temperature effects on oxygen quenching of protein phosphorescence, JACS 121 (1999) 8337-8344.
    • (1999) JACS , vol.121 , pp. 8337-8344
    • Strambini, G.B.1    Cioni, P.2
  • 77
    • 68249115779 scopus 로고    scopus 로고
    • Acrylamide quenching of Trp phosphorescence in liver alcohol dehydrogenase: Evidence of gated quencher penetration
    • G.B. Strambini, M. Gonnelli, Acrylamide quenching of Trp phosphorescence in liver alcohol dehydrogenase: evidence of gated quencher penetration, Biochemistry 48 (2009) 7482-7491.
    • (2009) Biochemistry , vol.48 , pp. 7482-7491
    • Strambini, G.B.1    Gonnelli, M.2
  • 78
    • 0026411154 scopus 로고
    • Copper protein structures
    • E.T. Adman, Copper protein structures, Adv. Protein Chem. 42 (1991) 145-197.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 145-197
    • Adman, E.T.1
  • 79
    • 0025953438 scopus 로고
    • Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0: A pH-induced conformational transition involves a peptide bond flip
    • H. Nar, A. Messerschmidt, R. Huber, M. van de Kamp, G.W. Canters, Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip, J. Mol. Biol. 221 (1991) 765-772. (Pubitemid 121003417)
    • (1991) Journal of Molecular Biology , vol.221 , Issue.3 , pp. 765-772
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De, K.M.4    Canters, G.W.5
  • 80
    • 0000092070 scopus 로고
    • Effect of temperature on the compressibility of native globular proteins
    • K. Gekko, Y. Hasegawa, Effect of temperature on the compressibility of native globular proteins, J. Phys. Chem. 93 (1989) 426-429.
    • (1989) J. Phys. Chem. , vol.93 , pp. 426-429
    • Gekko, K.1    Hasegawa, Y.2
  • 81
    • 0008047756 scopus 로고    scopus 로고
    • The hydration of globular proteins as derived from volume and compressibility measurements: Cross correlating thermodynamic and structural data
    • T.V. Chalikian, M. Totrov, R. Abagyan, K.J. Breslauer, The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data, J. Mol. Biol. 260 (1996) 588-603.
    • (1996) J. Mol. Biol. , vol.260 , pp. 588-603
    • Chalikian, T.V.1    Totrov, M.2    Abagyan, R.3    Breslauer, K.J.4
  • 82
    • 0033932840 scopus 로고    scopus 로고
    • Protein compressibility, dynamics, and pressure
    • D.P. Kharakoz, Protein compressibility, dynamics, and pressure, Biophys. J. 79 (2000) 511-525.
    • (2000) Biophys. J. , vol.79 , pp. 511-525
    • Kharakoz, D.P.1
  • 83
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
    • K. Gekko, S.N. Timasheff,Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures, Biochemistry 20 (1981) 4667-4676.
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 84
    • 0028071439 scopus 로고
    • Arc repressor will not denature under pressure in the absence of water
    • A.C. Oliveira, L.P. Gaspar, A.T. Da Poian, J.L. Silva, Arc repressor will not denature under pressure in the absence of water, J. Mol. Biol. 240 (1994) 184-187.
    • (1994) J. Mol. Biol. , vol.240 , pp. 184-187
    • Oliveira, A.C.1    Gaspar, L.P.2    Da Poian, A.T.3    Silva, J.L.4
  • 86
    • 0027250627 scopus 로고
    • Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration
    • DOI 10.1006/jmbi.1993.1417
    • P.L. Privalov, G.I. Makhatadze, Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration, J. Mol. Biol. 232 (1993) 660-679. (Pubitemid 23251185)
    • (1993) Journal of Molecular Biology , vol.232 , Issue.2 , pp. 660-679
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 87
    • 1142310676 scopus 로고    scopus 로고
    • Effects of Cavity-Forming Mutations on the Internal Dynamics of Azurin
    • P. Cioni, E. de Waal, G.W. Canters, G.B. Strambini, Effects of cavity-forming mutations on the internal dynamics of azurin, Biophys. J. 86 (2004) 1149-1159. (Pubitemid 38209558)
    • (2004) Biophysical Journal , vol.86 , Issue.2 , pp. 1149-1159
    • Cioni, P.1    De Waal, E.2    Canters, G.W.3    Strambini, G.B.4
  • 88
    • 0029916957 scopus 로고    scopus 로고
    • X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa
    • C. Hammann, A. Messerschmidt, R. Huber, H. Nar, G. Gilardi, G.W. Canters, X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa, J. Mol. Biol. 255 (1996) 362-366.
    • (1996) J. Mol. Biol. , vol.255 , pp. 362-366
    • Hammann, C.1    Messerschmidt, A.2    Huber, R.3    Nar, H.4    Gilardi, G.5    Canters, G.W.6
  • 90
    • 33751222894 scopus 로고    scopus 로고
    • Role of protein cavities on unfolding volume change and on internal dynamics under pressure
    • DOI 10.1529/biophysj.106.085670
    • P. Cioni, Role of protein cavities on unfolding volume change and on internal dynamics under pressure, Biophys. J. 91 (2006) 3390-3396. (Pubitemid 44788272)
    • (2006) Biophysical Journal , vol.91 , Issue.9 , pp. 3390-3396
    • Cioni, P.1
  • 91
    • 12344321689 scopus 로고    scopus 로고
    • Structural and energetic consequences of mutations in a solvated hydrophobic cavity
    • D.H. Adamek, L. Guerrero, M. Blaber, D.L. Caspar, Structural and energetic consequences of mutations in a solvated hydrophobic cavity, J. Mol. Biol. 346 (2005) 307-318.
    • (2005) J. Mol. Biol. , vol.346 , pp. 307-318
    • Adamek, D.H.1    Guerrero, L.2    Blaber, M.3    Caspar, D.L.4
  • 92
    • 0028921999 scopus 로고
    • Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR
    • J.A. Ernst, R.T. Clubb, H.X. Zhou, A.M. Gronenborn, G.M. Clore, Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR, Science 267 (1995) 1813-1817.
    • (1995) Science , vol.267 , pp. 1813-1817
    • Ernst, J.A.1    Clubb, R.T.2    Zhou, H.X.3    Gronenborn, A.M.4    Clore, G.M.5
  • 93
    • 0029561720 scopus 로고
    • Use of NMR to detect water within nonpolar protein cavities
    • DOI 10.1126/science.270.5243.1847
    • B.W. Matthews, A.G. Morton, F.W. Dahlquist, Use of NMR to detect water within nonpolar protein cavities, Science 270 (1995) 1847-1849. (Pubitemid 26007237)
    • (1995) Science , vol.270 , Issue.5243 , pp. 1847-1849
    • Matthews, B.W.1    Morton, A.G.2    Dahlquist, F.W.3
  • 94
    • 0034730423 scopus 로고    scopus 로고
    • Size versus polarizability in protein-ligand interactions: Binding of noble gases within engineered cavities in phage T4 lysozyme
    • M.L. Quillin, W.A. Breyer, I.J. Griswold, B.W. Matthews, Size versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 lysozyme, J. Mol. Biol. 302 (2000) 955-977.
    • (2000) J. Mol. Biol. , vol.302 , pp. 955-977
    • Quillin, M.L.1    Breyer, W.A.2    Griswold, I.J.3    Matthews, B.W.4
  • 95
    • 0029882171 scopus 로고    scopus 로고
    • Structural and energetic responses to cavity-creating mutations in hydrophobic cores: Observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities
    • DOI 10.1021/bi9524676
    • A.M. Buckle, P. Cramer, A.R. Fersht, Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities, Biochemistry 35 (1996) 4298-4305. (Pubitemid 26113489)
    • (1996) Biochemistry , vol.35 , Issue.14 , pp. 4298-4305
    • Buckle, A.M.1    Cramer, P.2    Fersht, A.R.3
  • 96
    • 61449156398 scopus 로고    scopus 로고
    • A review about nothing: Are apolar cavities in proteins really empty?
    • B.W. Matthews, L. Liu, A review about nothing: are apolar cavities in proteins really empty? Protein Sci. 18 (2009) 494-502.
    • (2009) Protein Sci. , vol.18 , pp. 494-502
    • Matthews, B.W.1    Liu, L.2
  • 98
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • A.E. Eriksson, W.A. Baase, X.J. Zhang, D.W. Heinz, M. Blaber, E.P. Baldwin, B.W. Matthews, Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect, Science 255 (1992) 178-183.
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Baase, W.A.2    Zhang, X.J.3    Heinz, D.W.4    Blaber, M.5    Baldwin, E.P.6    Matthews, B.W.7
  • 100
    • 0034651984 scopus 로고    scopus 로고
    • Water penetration and escape in proteins
    • DOI 10.1002/(SICI)1097-0134(20000215)38:3<261::AID-PROT3>3.0.CO;2-Q
    • A.E. Garcia, G. Hummer, Water penetration and escape in proteins, Proteins 38 (2000) 261-272. (Pubitemid 30084336)
    • (2000) Proteins: Structure, Function and Genetics , vol.38 , Issue.3 , pp. 261-272
    • Garcia, A.E.1    Hummer, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.