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Volumn 77, Issue 5, 1999, Pages 2801-2812

Effect of pressure on the tertiary structure and dynamics of folded basic pancreatic trypsin inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

APROTININ; GLOBULAR PROTEIN; PHENYLALANINE; TYROSINE;

EID: 0032705720     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77112-2     Document Type: Article
Times cited : (66)

References (45)
  • 2
    • 0031554921 scopus 로고    scopus 로고
    • Pressure-induced changes in the folded structure of lysozyme
    • Akasaka, K., T. Tezuka, and H. Yamada. 1997. Pressure-induced changes in the folded structure of lysozyme. J. Mol. Biol. 271:671-678.
    • (1997) J. Mol. Biol. , vol.271 , pp. 671-678
    • Akasaka, K.1    Tezuka, T.2    Yamada, H.3
  • 3
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri, A. S., D. P. Kinton, and R. A. Byrd. 1995. Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J. Am. Chem. Soc. 117:7566-7567.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Kinton, D.P.2    Byrd, R.A.3
  • 4
    • 0026795399 scopus 로고
    • Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures
    • Berndt, K. D., P. Guntert, L. P. M. Orbons, and K. Wuthrich. 1992. Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J. Mol. Biol. 227:757-775.
    • (1992) J. Mol. Biol. , vol.227 , pp. 757-775
    • Berndt, K.D.1    Guntert, P.2    Orbons, L.P.M.3    Wuthrich, K.4
  • 5
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing; application to proton correlation spectroscopy
    • Braunschweiler, L., and R. R. Ernst. 1983. Coherence transfer by isotropic mixing; application to proton correlation spectroscopy. J. Magn. Reson. 53:521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 6
    • 0027285706 scopus 로고
    • Dynamical properties of bovine pancreatic trypsin inhibitor from a molecular dynamics simulation at 5000 atm
    • Brunne, R. M., and W. F. van Gunsteren. 1993. Dynamical properties of bovine pancreatic trypsin inhibitor from a molecular dynamics simulation at 5000 atm. FEBS Lett. 323:215-217.
    • (1993) FEBS Lett. , vol.323 , pp. 215-217
    • Brunne, R.M.1    Van Gunsteren, W.F.2
  • 7
    • 0030298077 scopus 로고    scopus 로고
    • On volume changes accompanying conformational transitions of biopolymers
    • Chalikian, T. V., and K. J. Breslauer. 1996. On volume changes accompanying conformational transitions of biopolymers. Biopolymers. 39: 619-626.
    • (1996) Biopolymers , vol.39 , pp. 619-626
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 8
    • 0001612915 scopus 로고
    • Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 Å resolution
    • Deisenhofer, J., and W. Steigemann. 1975. Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 Å resolution. Acta Crystallogr. B. 31:238-250.
    • (1975) Acta Crystallogr. B , vol.31 , pp. 238-250
    • Deisenhofer, J.1    Steigemann, W.2
  • 9
    • 0022999267 scopus 로고
    • Compressibility-structure relationship of globular proteins
    • Gekko, K., and Y. Hasegawa. 1986. Compressibility-structure relationship of globular proteins. Biochemistry. 25:6563-6571.
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2
  • 10
    • 33845561444 scopus 로고
    • Compressibility of globular proteins in water at 25°C
    • Gekko, K., and H. Noguchi. 1979. Compressibility of globular proteins in water at 25°C. J. Phys. Chem. 83:2706-2714.
    • (1979) J. Phys. Chem. , vol.83 , pp. 2706-2714
    • Gekko, K.1    Noguchi, H.2
  • 11
    • 0029915110 scopus 로고    scopus 로고
    • Pressure-tuning the conformation of bovine pancreatic trypsin inhibitor studied by fourier-transform infrared spectroscopy
    • Goossens, K., L. Smeller, J. Frank, and K. Heremans. 1996. Pressure-tuning the conformation of bovine pancreatic trypsin inhibitor studied by Fourier-transform infrared spectroscopy. Eur. J. Biochem. 236:254-262.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 254-262
    • Goossens, K.1    Smeller, L.2    Frank, J.3    Heremans, K.4
  • 12
    • 0028220701 scopus 로고
    • The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
    • Gross, M., and R. Jaenicke. 1994. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221:617-630.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 617-630
    • Gross, M.1    Jaenicke, R.2
  • 13
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • Heremans, K., and L. Smeller. 1998. Protein structure and dynamics at high pressure. Biochim. Biophys. Acta. 1836:353-370.
    • (1998) Biochim. Biophys. Acta. , vol.1836 , pp. 353-370
    • Heremans, K.1    Smeller, L.2
  • 14
    • 0032197513 scopus 로고    scopus 로고
    • High pressure nmr study of a small protein, gurmarin
    • Inoue, K., H. Yamada, T. Imoto, and K. Akasaka. 1998. High pressure NMR study of a small protein, gurmarin. J. Biomol. NMR. 12:535-541.
    • (1998) J. Biomol. NMR , vol.12 , pp. 535-541
    • Inoue, K.1    Yamada, H.2    Imoto, T.3    Akasaka, K.4
  • 16
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, T., B. H. Meier, P. Bachmann, and R. R. Ernst. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71:4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, T.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 17
    • 0028226052 scopus 로고
    • High-pressure NMR spectroscopy of proteins and membranes
    • Jonas, A., and J. Jonas. 1994. High-pressure NMR spectroscopy of proteins and membranes. Annu. Rev. Biophys. Biomol. Struct. 23:287-318.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 287-318
    • Jonas, A.1    Jonas, J.2
  • 18
    • 0026785575 scopus 로고
    • Molecular dynamics simulation of solvated protein at high pressure
    • Kitchen, D. B., L. H. Reed, and R. M. Levy. 1992. Molecular dynamics simulation of solvated protein at high pressure. Biochemistry. 31: 10083-10093.
    • (1992) Biochemistry , vol.31 , pp. 10083-10093
    • Kitchen, D.B.1    Reed, L.H.2    Levy, R.M.3
  • 19
    • 0030589519 scopus 로고    scopus 로고
    • Properties of the protein matrix revealed by the free energy of cavity formation
    • Kocher, J. P., M. Prevost, S. J. Wodak, and B. Lee. 1996. Properties of the protein matrix revealed by the free energy of cavity formation. Structure. 4:1517-1529.
    • (1996) Structure , vol.4 , pp. 1517-1529
    • Kocher, J.P.1    Prevost, M.2    Wodak, S.J.3    Lee, B.4
  • 20
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis for macromolecular structures
    • Koradi, R., M. Billeter, and K. Wuthrich. 1996. MOLMOL: a program for display and analysis for macromolecular structures. J. Mol. Graph. 14:51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 21
    • 0023644307 scopus 로고
    • Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres
    • Kundrot, C. E., and F. M. Richards. 1987. Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. J. Mol. Biol 193:157-170.
    • (1987) J. Mol. Biol , vol.193 , pp. 157-170
    • Kundrot, C.E.1    Richards, F.M.2
  • 22
    • 0032477750 scopus 로고    scopus 로고
    • Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor
    • Li, H., H. Yamada, and K. Akasaka. 1998. Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor. Biochemistry. 37:1167-1173.
    • (1998) Biochemistry , vol.37 , pp. 1167-1173
    • Li, H.1    Yamada, H.2    Akasaka, K.3
  • 24
    • 49049150378 scopus 로고
    • Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclear spins
    • Macura, C., Y. Huang, D. Suter, and R. R. Ernst. 1981. Two-dimensional chemical exchange and cross-relaxation spectroscopy of coupled nuclear spins. J. Magn. Reson. 43:259-281.
    • (1981) J. Magn. Reson. , vol.43 , pp. 259-281
    • Macura, C.1    Huang, Y.2    Suter, D.3    Ernst, R.R.4
  • 25
    • 0021114895 scopus 로고
    • Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of H-1-H-1 spin-spin coupling-constants in proteins
    • Marion, D., and K. Wuthrich. 1983. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of H-1-H-1 spin-spin coupling-constants in proteins. Biochem. Biophys. Res. Common. 113:967-974.
    • (1983) Biochem. Biophys. Res. Common. , vol.113 , pp. 967-974
    • Marion, D.1    Wuthrich, K.2
  • 27
    • 36849149270 scopus 로고
    • Protein structure. New light on old defects
    • Pain, R. H. 1987. Protein structure. New light on old defects. Nature. 326:247.
    • (1987) Nature , vol.326 , pp. 247
    • Pain, R.H.1
  • 29
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., V. Saudek, and V. Sklenar. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 30
    • 0032574699 scopus 로고    scopus 로고
    • Pressure denaturation of proteins: Evaluation of compressibility effects
    • Prehoda, K. E., E. S. Mooberry, and J. L. Markley. 1998. Pressure denaturation of proteins: evaluation of compressibility effects. Biochemistry. 37:5785-5790.
    • (1998) Biochemistry , vol.37 , pp. 5785-5790
    • Prehoda, K.E.1    Mooberry, E.S.2    Markley, J.L.3
  • 31
    • 0347358202 scopus 로고    scopus 로고
    • Theories of chemical shift anisotropies in proteins and nucleic acids
    • Sitkoff, D., and D. A. Case. 1998. Theories of chemical shift anisotropies in proteins and nucleic acids. Prog. Nucl. Magn. Reson. Spectrosc. 32:165-190.
    • (1998) Prog. Nucl. Magn. Reson. Spectrosc. , vol.32 , pp. 165-190
    • Sitkoff, D.1    Case, D.A.2
  • 32
    • 0001350902 scopus 로고
    • Gradient-tailored water suppression for H-1-N-15 HSQC experiments optimized to retain full sensitivity
    • Sklenar, V., M. Piotto, R. Leppik, and V. Saudek. 1993. Gradient-tailored water suppression for H-1-N-15 HSQC experiments optimized to retain full sensitivity. J. Magn. Reson., Ser. A. 102:241-245.
    • (1993) J. Magn. Reson., Ser. A. , vol.102 , pp. 241-245
    • Sklenar, V.1    Piotto, M.2    Leppik, R.3    Saudek, V.4
  • 33
    • 0029024519 scopus 로고
    • Pressure- and thermally induced reversible changes in the secondary structure of ribonuclease A studied by FT-IR spectroscopy
    • Takeda, N., M. Kato, and Y. Taniguchi. 1995. Pressure- and thermally induced reversible changes in the secondary structure of ribonuclease A studied by FT-IR spectroscopy. Biochemistry. 34:5980-5987.
    • (1995) Biochemistry , vol.34 , pp. 5980-5987
    • Takeda, N.1    Kato, M.2    Taniguchi, Y.3
  • 34
    • 0031604560 scopus 로고    scopus 로고
    • Pressure-induced structural rearrangements of bovine pancreatic trypsin inhibitor studied by FTIR spectroscopy
    • Takeda, N., K. Nakano, M. Kato, and M. Taniguch. 1998. Pressure-induced structural rearrangements of bovine pancreatic trypsin inhibitor studied by FTIR spectroscopy. Biospectroscopy. 4:209-216.
    • (1998) Biospectroscopy , vol.4 , pp. 209-216
    • Takeda, N.1    Nakano, K.2    Kato, M.3    Taniguch, M.4
  • 35
    • 0029963645 scopus 로고    scopus 로고
    • High-resolution triple-resonance NMR spectroscopy of a novel calmodulin-peptide complex at kilobar pressure
    • Urbauer, J. L., M. R. Ehrhardt, R. J. Bieber, P. F. Flynn, and A. J. Wand. 1996. High-resolution triple-resonance NMR spectroscopy of a novel calmodulin-peptide complex at kilobar pressure. J. Am. Chem. Soc. 118:11329-11330.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11329-11330
    • Urbauer, J.L.1    Ehrhardt, M.R.2    Bieber, R.J.3    Flynn, P.F.4    Wand, A.J.5
  • 36
    • 0019318643 scopus 로고
    • 1H-NMR at variable pressure
    • 1H-NMR at variable pressure. FEBS Lett. 112:280-284.
    • (1980) FEBS Lett. , vol.112 , pp. 280-284
    • Wagner, G.1
  • 37
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner, G., W. Braun, T. F. Havel, T. Schumann, N. Go, and K. Wüthrich. 1987. Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196:611-639.
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schumann, T.4    Go, N.5    Wüthrich, K.6
  • 38
    • 0020712468 scopus 로고
    • The effect of high pressure upon proteins and other biomolecules
    • Weber, G., and H. G. Drickamer. 1983. The effect of high pressure upon proteins and other biomolecules. Q. Rev. Biophys. 16:89-112.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 89-112
    • Weber, G.1    Drickamer, H.G.2
  • 39
    • 44949269218 scopus 로고
    • Empirical comparisons of models for chemical-shift calculation in proteins
    • Williamson, M. P., and T. Asakura. 1993. Empirical comparisons of models for chemical-shift calculation in proteins. J. Magn. Reson., Ser. B. 101:63-71.
    • (1993) J. Magn. Reson., Ser. B. , vol.101 , pp. 63-71
    • Williamson, M.P.1    Asakura, T.2
  • 41
    • 0023120307 scopus 로고
    • Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and x-ray refinement of crystal form II
    • Wlodawer, A., J. Walter, R. Huber, and L. Sjolin. 1984. Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and x-ray refinement of crystal form II. J. Mol. Biol. 193:145-156.
    • (1984) J. Mol. Biol. , vol.193 , pp. 145-156
    • Wlodawer, A.1    Walter, J.2    Huber, R.3    Sjolin, L.4
  • 44
    • 0016056448 scopus 로고
    • Pressure-resisting glass cell for high pressure, high resolution NMR measurement
    • Yamada, H. 1974. Pressure-resisting glass cell for high pressure, high resolution NMR measurement. Rev. Sci. Instrum. 45:640-642.
    • (1974) Rev. Sci. Instrum. , vol.45 , pp. 640-642
    • Yamada, H.1
  • 45
    • 0027179514 scopus 로고
    • Conformational deformation in deoxymyoglobin in hydrostatic pressure
    • Yamato, T., J. Higo, Y. Seno, and N. Go. 1993. Conformational deformation in deoxymyoglobin in hydrostatic pressure. Proteins: Struct., Funct., Genet. 16:327-340.
    • (1993) Proteins: Struct., Funct., Genet. , vol.16 , pp. 327-340
    • Yamato, T.1    Higo, J.2    Seno, Y.3    Go, N.4


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