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Volumn 4, Issue 3, 1998, Pages 209-216

Pressure-induced structural rearrangements of bovine pancreatic trypsin inhibitor studied by FTIR spectroscopy

Author keywords

Bovine pancreatic trypsin inhibitor; FTIR spectroscopy; High pressure; Hydrogen deuterium exchange

Indexed keywords

APROTININ; DEUTERIUM OXIDE;

EID: 0031604560     PISSN: 10754261     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1520-6343(1998)4:3<209::aid-bspy6>3.0.co;2-z     Document Type: Article
Times cited : (16)

References (32)
  • 1
    • 0029024519 scopus 로고
    • Pressure and thermally-induced reversible changes in the secondary structure of ribonuclease A studied by FTIR spectroscopy
    • N. Takeda, M. Kato, and Y. Taniguchi, "Pressure and thermally-induced reversible changes in the secondary structure of ribonuclease A studied by FTIR spectroscopy," Biochemistry, 34, 5980-5987 (1995).
    • (1995) Biochemistry , vol.34 , pp. 5980-5987
    • Takeda, N.1    Kato, M.2    Taniguchi, Y.3
  • 2
    • 84984234595 scopus 로고
    • Pressure-induced secondary structure changes of ribonuclease A and ribonuclease S studied by FTIR spectroscopy
    • N. Takeda, M. Kato, and Y. Taniguchi, "Pressure-induced secondary structure changes of ribonuclease A and ribonuclease S studied by FTIR spectroscopy," Biospectroscopy, 1, 207-216 (1995).
    • (1995) Biospectroscopy , vol.1 , pp. 207-216
    • Takeda, N.1    Kato, M.2    Taniguchi, Y.3
  • 3
    • 0026781884 scopus 로고
    • High resolution NMR study of the pressure-induced unfolding of lysozyme
    • S. D. Samarasinghe, D. M. Campbell, A. Jonas, and J. Jonas, "High resolution NMR study of the pressure-induced unfolding of lysozyme," Biochemistry, 31, 7773-7778 (1992).
    • (1992) Biochemistry , vol.31 , pp. 7773-7778
    • Samarasinghe, S.D.1    Campbell, D.M.2    Jonas, A.3    Jonas, J.4
  • 4
    • 0029040518 scopus 로고
    • NMR study of the cold, heat, and pressure unfolding of ribonuclease A
    • J. Zhang, X. Peng, A. Jonas, and J. Jonas, "NMR study of the cold, heat, and pressure unfolding of ribonuclease A," Biochemistry, 34, 8631-8641 (1995).
    • (1995) Biochemistry , vol.34 , pp. 8631-8641
    • Zhang, J.1    Peng, X.2    Jonas, A.3    Jonas, J.4
  • 5
    • 0026785575 scopus 로고
    • Molecular dynamics simulation of solvated protein at high pressure
    • D. B. Kitchen, L. H. Reed, and R. M. Levy, "Molecular dynamics simulation of solvated protein at high pressure," Biochemistry, 31, 10083-10093 (1992).
    • (1992) Biochemistry , vol.31 , pp. 10083-10093
    • Kitchen, D.B.1    Reed, L.H.2    Levy, R.M.3
  • 6
    • 0342325481 scopus 로고
    • Pressure inactivation of α-chymotrypsin
    • Y. Taniguchi and K. Suzuki, "Pressure inactivation of α-chymotrypsin," J. Phys. Chem., 87, 5185-5193 (1983).
    • (1983) J. Phys. Chem. , vol.87 , pp. 5185-5193
    • Taniguchi, Y.1    Suzuki, K.2
  • 7
    • 0028905560 scopus 로고
    • Evidence for a molten globule-like transition state in protein folding from determination of activation volumes
    • G. J. A. Vidugiris, J. L. Markley, and C. A. Royer, "Evidence for a molten globule-like transition state in protein folding from determination of activation volumes," Biochemistry, 34, 4909-4912 (1995).
    • (1995) Biochemistry , vol.34 , pp. 4909-4912
    • Vidugiris, G.J.A.1    Markley, J.L.2    Royer, C.A.3
  • 9
    • 0023626273 scopus 로고
    • Protein folding: Hypotheses and experiments
    • O. B. Ptitsyn, "Protein folding: hypotheses and experiments," J. Protein Chem., 6, 273-293 (1987).
    • (1987) J. Protein Chem. , vol.6 , pp. 273-293
    • Ptitsyn, O.B.1
  • 10
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperatively of globular-protein structure
    • K. Kuwajima, "The molten globule state as a clue for understanding the folding and cooperatively of globular-protein structure," Proteins: Struct., Funct., Genet., 6, 87-103 (1989).
    • (1989) Proteins: Struct., Funct., Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 11
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • W. K. Surewicz, H. H. Mantsch, and D. Chapman, "Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment," Biochemistry, 32, 389-394 (1993).
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 12
    • 0001090283 scopus 로고
    • Crystalline quartz as an internal pressure calibrant for high pressure infrared spectroscopy
    • P. T. T. Wong, D. J. Moffatt, and F. L. Baudais, "Crystalline quartz as an internal pressure calibrant for high pressure infrared spectroscopy," Appl. Spectrosc., 39, 733-735 (1985).
    • (1985) Appl. Spectrosc. , vol.39 , pp. 733-735
    • Wong, P.T.T.1    Moffatt, D.J.2    Baudais, F.L.3
  • 13
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • S. Krimm and J. Bandekar, "Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins," Adv. Protein Chem., 38, 181-364 (1986).
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 14
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • D. M. Byler and H. Susi, "Examination of the secondary structure of proteins by deconvolved FTIR spectra," Biopolymers, 25, 487-496 (1986).
    • (1986) Biopolymers , vol.25 , pp. 487-496
    • Byler, D.M.1    Susi, H.2
  • 15
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • W. K. Surewicz and H. H. Mantsch, "New insight into protein secondary structure from resolution-enhanced infrared spectra," Biochim. Biophys. Acta, 952, 115-130 (1988).
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 16
    • 0025357111 scopus 로고
    • Protein secondary structures in water form second-derivative amide I infrared spectra
    • A. Dong, P. Huang, and W. S. Caughey, "Protein secondary structures in water form second-derivative amide I infrared spectra," Biochemistry, 29, 3303-3308 (1990).
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 17
    • 0025880710 scopus 로고
    • 10- and α-helices and β-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy
    • 10- and α-helices and β-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy," Biochemistry, 30, 6541-6548 (1991).
    • (1991) Biochemistry , vol.30 , pp. 6541-6548
    • Kennedy, D.F.1    Crisma, M.2    Toniolo, C.3    Chapman, D.4
  • 18
    • 0023120307 scopus 로고
    • Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor
    • A. Wlodawer, J. Deisenhofer, and R. Huber, "Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor," J. Mol. Biol., 193, 145-156 (1987).
    • (1987) J. Mol. Biol. , vol.193 , pp. 145-156
    • Wlodawer, A.1    Deisenhofer, J.2    Huber, R.3
  • 20
    • 0022399120 scopus 로고
    • Amide proton exchange in proteins by EX1 kinetics: Studies of the basic pancreatic trypsin inhibitor at variable pH and temperature
    • H. Roder, G. Wagner, and K. Wuthrich, "Amide proton exchange in proteins by EX1 kinetics: Studies of the basic pancreatic trypsin inhibitor at variable pH and temperature," Biochemistry, 24, 7396-7407 (1985).
    • (1985) Biochemistry , vol.24 , pp. 7396-7407
    • Roder, H.1    Wagner, G.2    Wuthrich, K.3
  • 21
    • 0026647269 scopus 로고
    • Comparison of hydrogen exchange rates for bovine pancreatic trypsin inhibitor in crystals and in solution
    • W. Gallagher, F. Tao, and C. Woodward, "Comparison of hydrogen exchange rates for bovine pancreatic trypsin inhibitor in crystals and in solution," Biochemistry, 31, 4673-4680 (1992).
    • (1992) Biochemistry , vol.31 , pp. 4673-4680
    • Gallagher, W.1    Tao, F.2    Woodward, C.3
  • 22
    • 0027504749 scopus 로고
    • Hydrogen exchange identifies native-state motional domains important in protein folding
    • K.-S. Kim, J. A. Fuchs, and C. K. Woodward, "Hydrogen exchange identifies native-state motional domains important in protein folding," Biochemistry, 32, 9600-9608 (1993).
    • (1993) Biochemistry , vol.32 , pp. 9600-9608
    • Kim, K.-S.1    Fuchs, J.A.2    Woodward, C.K.3
  • 23
    • 0016797947 scopus 로고
    • Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water
    • Y. N. Chirgadze, O. V. Fedorov, and N. P. Trushina, "Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water," Biopolymers, 14, 679-694 (1975).
    • (1975) Biopolymers , vol.14 , pp. 679-694
    • Chirgadze, Y.N.1    Fedorov, O.V.2    Trushina, N.P.3
  • 24
    • 0000340228 scopus 로고
    • Infrared and Raman spectra of N-acetyl-L-amino acid methylamides with aromatic side groups
    • H. Matsuura, K. Hasegawa, and T. Miyazawa, "Infrared and Raman spectra of N-acetyl-L-amino acid methylamides with aromatic side groups," Spectrochim. Acta, 42A, 1181-1192 (1986).
    • (1986) Spectrochim. Acta , vol.42 A , pp. 1181-1192
    • Matsuura, H.1    Hasegawa, K.2    Miyazawa, T.3
  • 25
    • 0025007841 scopus 로고
    • Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy
    • W. K. Surewicz, J. J. Leddy, and H. H. Mantsch, "Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy," Biochemistry, 29, 8106-8111 (1990).
    • (1990) Biochemistry , vol.29 , pp. 8106-8111
    • Surewicz, W.K.1    Leddy, J.J.2    Mantsch, H.H.3
  • 26
    • 0025841667 scopus 로고
    • Membrane binding induces destabilization of cytochrome c structure
    • A. Muga, H. H. Mantsch, and W. K. Surewicz, "Membrane binding induces destabilization of cytochrome c structure," Biochemistry, 30, 7219-7224 (1991).
    • (1991) Biochemistry , vol.30 , pp. 7219-7224
    • Muga, A.1    Mantsch, H.H.2    Surewicz, W.K.3
  • 27
    • 0026642332 scopus 로고
    • Aggregation of chymotrypsinogen: Portrait by infrared spectroscopy
    • A. A. Ismail, H. H. Mantsch, and P. T. T. Wong, "Aggregation of chymotrypsinogen: Portrait by infrared spectroscopy ,"Biochim. Biophys. Acta, 1121, 183-188 (1992).
    • (1992) ,Biochim. Biophys. Acta , vol.1121 , pp. 183-188
    • Ismail, A.A.1    Mantsch, H.H.2    Wong, P.T.T.3
  • 28
    • 0027469789 scopus 로고
    • Secondary structure and temperature behavior the acetylcholine receptor by Fourier transform infrared spectroscopy
    • D. Naumann, C. Schultz, U. G. Tschelnokow, and F. Hucho, "Secondary structure and temperature behavior the acetylcholine receptor by Fourier transform infrared spectroscopy," Biochemistry, 32, 3162-3168 (1993).
    • (1993) Biochemistry , vol.32 , pp. 3162-3168
    • Naumann, D.1    Schultz, C.2    Tschelnokow, U.G.3    Hucho, F.4
  • 29
    • 0027273987 scopus 로고
    • Aggregation and denaturation of apomyoglobin in aqueous urea solution
    • L. R. De Young, K. A. Dill, and A. L. Fink, "Aggregation and denaturation of apomyoglobin in aqueous urea solution," Biochemistry, 32, 3877-3886 (1993).
    • (1993) Biochemistry , vol.32 , pp. 3877-3886
    • De Young, L.R.1    Dill, K.A.2    Fink, A.L.3
  • 30
    • 0020493395 scopus 로고
    • Hydrogen exchange and the dynamic structures of proteins
    • C. Woodward, I. Simon, and E. T. Chsen, "Hydrogen exchange and the dynamic structures of proteins," Mol. Cell. Biochem., 48, 135-160 (1982).
    • (1982) Mol. Cell. Biochem. , vol.48 , pp. 135-160
    • Woodward, C.1    Simon, I.2    Chsen, E.T.3
  • 31
    • 0020711969 scopus 로고
    • Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes
    • G. Wagner, "Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes," Quart. Rev. Biophys., 16, 1-57 (1983).
    • (1983) Quart. Rev. Biophys. , vol.16 , pp. 1-57
    • Wagner, G.1
  • 32
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • S. W. Englander and N. R. Kallenbach, "Hydrogen exchange and structural dynamics of proteins and nucleic acids," Quart. Rev. Biophys., 16, 521-655 (1984).
    • (1984) Quart. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2


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