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Volumn 12, Issue 4, 2003, Pages 717-724

Structural dissection of alkaline-denatured pepsin

Author keywords

Denaturation; Limited proteolysis; Partially folded state; Pepsin; Zymogen

Indexed keywords

PEPSIN A;

EID: 0037378360     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0219903     Document Type: Article
Times cited : (33)

References (43)
  • 1
    • 0017878090 scopus 로고
    • Thermodynamics of the denaturation of pepsinogen by urea
    • Ahmad, F. and McPhie, P. 1978a. Thermodynamics of the denaturation of pepsinogen by urea. Biochemistry 17: 241-246.
    • (1978) Biochemistry , vol.17 , pp. 241-246
    • Ahmad, F.1    McPhie, P.2
  • 2
    • 0018186127 scopus 로고
    • The denaturation of covalently inhibited swine pepsin
    • -. 1978b. The denaturation of covalently inhibited swine pepsin. Int. J. Pept. Protein Res. 12: 155-163.
    • (1978) Int. J. Pept. Protein Res. , vol.12 , pp. 155-163
  • 3
    • 0031436142 scopus 로고    scopus 로고
    • Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction
    • Aoki, K., Taguchi, H., Shindo, Y., Yoshida, M., Ogasahara, K., Yutani, K., and Tanaka, N. 1997. Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction. J. Biol. Chem. 272: 32158-32162.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32158-32162
    • Aoki, K.1    Taguchi, H.2    Shindo, Y.3    Yoshida, M.4    Ogasahara, K.5    Yutani, K.6    Tanaka, N.7
  • 5
    • 0024533979 scopus 로고
    • Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin
    • Baum, J., Dobson, C.M., Evans, P.A. and Hanley, C. 1989. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin. Biochemistry 28: 7-13.
    • (1989) Biochemistry , vol.28 , pp. 7-13
    • Baum, J.1    Dobson, C.M.2    Evans, P.A.3    Hanley, C.4
  • 6
    • 0000684595 scopus 로고
    • Structure of a pepsin/renin inhibitor complex reveals a novel crystal packing induced by minor chemical alterations in the inhibitor
    • Chen, L., Erickson, J.W., Rydel, T.J., Park, C.H., Neidhart, D., Luly, J., and Abad-Zapatero, C. 1992. Structure of a pepsin/renin inhibitor complex reveals a novel crystal packing induced by minor chemical alterations in the inhibitor. Acta. Crystallogr. B 48: 476-488.
    • (1992) Acta. Crystallogr. B , vol.48 , pp. 476-488
    • Chen, L.1    Erickson, J.W.2    Rydel, T.J.3    Park, C.H.4    Neidhart, D.5    Luly, J.6    Abad-Zapatero, C.7
  • 7
    • 0025297753 scopus 로고
    • X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 Å resolution
    • Cooper, J.B., Khan, G., Taylor, G., Tickle, I.J., and Blundell, T.L. 1990. X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 Å resolution. J. Mol. Biol. 214: 199-222.
    • (1990) J. Mol. Biol , vol.214 , pp. 199-222
    • Cooper, J.B.1    Khan, G.2    Taylor, G.3    Tickle, I.J.4    Blundell, T.L.5
  • 9
    • 0034021377 scopus 로고    scopus 로고
    • Two energetically disparate folding pathways of α-lytic protease share a single transition state
    • Derman, A.L. and Agard, D.A. 2000. Two energetically disparate folding pathways of α-lytic protease share a single transition state. Nat. Struct. Biol. 7: 394-397.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 394-397
    • Derman, A.L.1    Agard, D.A.2
  • 10
    • 0025856806 scopus 로고
    • Denatured states of proteins
    • Dill, K.A. and Shortle, D. 1991. Denatured states of proteins. Annu. Rev. Biochem. 60: 795-825.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 11
    • 0034912536 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states
    • Dyson, H.J. and Wright, P.E. 2001. Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states. Methods Enzymol. 339: 258-270.
    • (2001) Methods Enzymol. , vol.339 , pp. 258-270
    • Dyson, H.J.1    Wright, P.E.2
  • 12
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. 1967. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6: 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 13
    • 0029019483 scopus 로고
    • Pro-sequence-assisted protein folding
    • Eder, J. and Fersht, A.R. 1995. Pro-sequence-assisted protein folding. Mol. Microbiol. 16: 609-614.
    • (1995) Mol. Microbiol. , vol.16 , pp. 609-614
    • Eder, J.1    Fersht, A.R.2
  • 15
    • 0012495198 scopus 로고
    • Pepsin
    • ed. P.D. Boyer. Academic Press, New York
    • Fruton, J.S. 1960. Pepsin. In The enzymes III. (ed. P.D. Boyer), pp. 119-164. Academic Press, New York.
    • (1960) The Enzymes III , pp. 119-164
    • Fruton, J.S.1
  • 16
    • 0035987666 scopus 로고    scopus 로고
    • A history of pepsin and related enzymes
    • -. 2002. A history of pepsin and related enzymes. Q. Rev. Biol. 77: 127-147.
    • (2002) Q. Rev. Biol. , vol.77 , pp. 127-147
  • 17
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C. and von Hipple, P. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182: 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hipple, P.2
  • 18
    • 0023644876 scopus 로고
    • Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli
    • Ikemura, H., Takagi, H., and Inoue, M. 1987. Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli. J. Biol. Chem. 262: 7859-7864.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7859-7864
    • Ikemura, H.1    Takagi, H.2    Inoue, M.3
  • 19
    • 0029893286 scopus 로고    scopus 로고
    • The methanol-induced globular and expanded denatured states of cytochrome c: A study by CD fluorescence. NMR and small-angle X-ray scattering
    • Kamatari, Y.O., Konno, T., Kataoka, M., and Akasaka, K. 1996. The methanol-induced globular and expanded denatured states of cytochrome c: A study by CD fluorescence, NMR and small-angle X-ray scattering. J. Mol. Biol. 259: 512-523.
    • (1996) J. Mol. Biol. , vol.259 , pp. 512-523
    • Kamatari, Y.O.1    Konno, T.2    Kataoka, M.3    Akasaka, K.4
  • 20
    • 0032918979 scopus 로고    scopus 로고
    • The compact and expanded denatured conformations of apomyoglobin in the methanol-water solvent
    • Kamatari, Y.O., Ohji, S., Konno, T., Seki, Y., Soda, K., Kataoka, M., and Akasaka, K. 1999. The compact and expanded denatured conformations of apomyoglobin in the methanol-water solvent. Protein Sci. 8: 873-882.
    • (1999) Protein Sci. , vol.8 , pp. 873-882
    • Kamatari, Y.O.1    Ohji, S.2    Konno, T.3    Seki, Y.4    Soda, K.5    Kataoka, M.6    Akasaka, K.7
  • 21
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure. Pattern recognition of hydrogen bonded and geometrical features
    • Kasch, W. and Sander, C. 1983. Dictionary of protein secondary structure. Pattern recognition of hydrogen bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kasch, W.1    Sander, C.2
  • 22
    • 0035957228 scopus 로고    scopus 로고
    • Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
    • Khurana, R., Gillespie, J.R., Talapatra, A., Minert, L.J., Ionescu-Zanetti, C., Millett, I., and Fink, A.L. 2001. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40: 3525-3535.
    • (2001) Biochemistry , vol.40 , pp. 3525-3535
    • Khurana, R.1    Gillespie, J.R.2    Talapatra, A.3    Minert, L.J.4    Ionescu-Zanetti, C.5    Millett, I.6    Fink, A.L.7
  • 23
    • 0035916279 scopus 로고    scopus 로고
    • Amyloid-induced aggregation and precipitation of soluble proteins: An electrostatic contribution of the Alzheimer's β(25-35) amyloid fibril
    • Konno, T. 2001. Amyloid-induced aggregation and precipitation of soluble proteins: An electrostatic contribution of the Alzheimer's β(25-35) amyloid fibril. Biochemistry 40: 2148-2154.
    • (2001) Biochemistry , vol.40 , pp. 2148-2154
    • Konno, T.1
  • 24
    • 0034636112 scopus 로고    scopus 로고
    • A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein
    • Konno, T., Kamatari, Y.O., Tanaka, N., Kamikubo, H., Dobson, C.M., and Nagayama, K. 2000. A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein. Biochemistry 39: 4182-4190.
    • (2000) Biochemistry , vol.39 , pp. 4182-4190
    • Konno, T.1    Kamatari, Y.O.2    Tanaka, N.3    Kamikubo, H.4    Dobson, C.M.5    Nagayama, K.6
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 26
    • 0034866090 scopus 로고    scopus 로고
    • In vitro refolding of porcine pepsin immobilized on agarose beads
    • Kurimoto, E., Harada, T., Akiyama, A., Sakai, T., and Kato, K. 2001. In vitro refolding of porcine pepsin immobilized on agarose beads. J. Biochem. (Tokyo). 130: 295-297.
    • (2001) J. Biochem. (Tokyo) , vol.130 , pp. 295-297
    • Kurimoto, E.1    Harada, T.2    Akiyama, A.3    Sakai, T.4    Kato, K.5
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0027318025 scopus 로고
    • Conformational instability of the N- and C-terminal lobes of porcine pepsin in neutral and alkaline solutions
    • Lin, X., Loy, J.A., Sussman, F., and Tang, J. 1993. Conformational instability of the N- and C-terminal lobes of porcine pepsin in neutral and alkaline solutions. Protein Sci. 2: 1383-1390.
    • (1993) Protein Sci. , vol.2 , pp. 1383-1390
    • Lin, X.1    Loy, J.A.2    Sussman, F.3    Tang, J.4
  • 29
    • 0028203899 scopus 로고
    • Unfolding studies of the protease domain of urokinase-type plasminogen activator: The existence of partly folded states and stable subdomains
    • Nowak, U.K., Cooper, A., Saunders, D., Smith, R.A., and Dobson, C.M. 1994. Unfolding studies of the protease domain of urokinase-type plasminogen activator: The existence of partly folded states and stable subdomains. Biochemistry 33: 2951-2960.
    • (1994) Biochemistry , vol.33 , pp. 2951-2960
    • Nowak, U.K.1    Cooper, A.2    Saunders, D.3    Smith, R.A.4    Dobson, C.M.5
  • 31
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar V. 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
  • 32
    • 0030976078 scopus 로고    scopus 로고
    • The importance of being unfolded
    • Plaxco, K.W. and Gross, M. 1997. The importance of being unfolded. Nature 386: 657-659.
    • (1997) Nature , vol.386 , pp. 657-659
    • Plaxco, K.W.1    Gross, M.2
  • 35
    • 0032211774 scopus 로고    scopus 로고
    • Mechanism of activation of the gastric aspartic proteinases: Pepsinogen, progastricsin and prochymosin
    • Richter, C., Tanaka, T. and Yada, R.Y. 1998. Mechanism of activation of the gastric aspartic proteinases: Pepsinogen, progastricsin and prochymosin. Biochem. J. 335: 481-490.
    • (1998) Biochem. J. , vol.335 , pp. 481-490
    • Richter, C.1    Tanaka, T.2    Yada, R.Y.3
  • 36
    • 0025354599 scopus 로고
    • Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 Å resolution
    • Sielecki, A.R., Fedorov, A.A., Boodhoo, A., Andreeva, N.S., and James, N.G. 1990. Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 Å resolution. J. Mol. Biol. 214: 143-170.
    • (1990) J. Mol. Biol. , vol.214 , pp. 143-170
    • Sielecki, A.R.1    Fedorov, A.A.2    Boodhoo, A.3    Andreeva, N.S.4    James, N.G.5
  • 37
    • 0030320442 scopus 로고    scopus 로고
    • The concept of a random coil. Residual structure in peptides and denatured proteins
    • Smith, L.J., Fiebig, K.M., Schwalbe, H., and Dobson, C.M. 1996. The concept of a random coil. Residual structure in peptides and denatured proteins. Fold Des. 1: R95-R106.
    • (1996) Fold Des. , vol.1
    • Smith, L.J.1    Fiebig, K.M.2    Schwalbe, H.3    Dobson, C.M.4
  • 38
    • 0032558779 scopus 로고    scopus 로고
    • Unfolded conformations of α-lytic protease are more stable than its native state
    • Sohl, J.L., Jaswal, S.S., and Agard, D.A. 1998. Unfolded conformations of α-lytic protease are more stable than its native state. Nature 395: 817-819.
    • (1998) Nature , vol.395 , pp. 817-819
    • Sohl, J.L.1    Jaswal, S.S.2    Agard, D.A.3
  • 39
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. and Woody, R.W. 2000. Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem 287: 252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 40
    • 0035183895 scopus 로고    scopus 로고
    • N-terminal portion acts as an initiator of the inactivation of pepsin at neutral pH
    • Tanaka, T. and Yada, R.Y. 2001. N-terminal portion acts as an initiator of the inactivation of pepsin at neutral pH. Protein Eng. 14: 669-674.
    • (2001) Protein Eng. , vol.14 , pp. 669-674
    • Tanaka, T.1    Yada, R.Y.2
  • 41
    • 0034601786 scopus 로고    scopus 로고
    • Pressure effect on the conformational fluctuation of apomyoglobin in the native state
    • Tanaka, N., Ikeda, C., Kanaori, K., Hiraga, K., Konno, T., and Kunigi, S. 2000. Pressure effect on the conformational fluctuation of apomyoglobin in the native state. Biochemistry 39: 12063-12068.
    • (2000) Biochemistry , vol.39 , pp. 12063-12068
    • Tanaka, N.1    Ikeda, C.2    Kanaori, K.3    Hiraga, K.4    Konno, T.5    Kunigi, S.6
  • 42
    • 0024409494 scopus 로고
    • Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process
    • Zhu, X.L., Ohta, Y., Jordan, F., and Inouye, M. 1989. Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Nature 339: 483-484.
    • (1989) Nature , vol.339 , pp. 483-484
    • Zhu, X.L.1    Ohta, Y.2    Jordan, F.3    Inouye, M.4
  • 43
    • 0035839035 scopus 로고    scopus 로고
    • Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain
    • Zurdo, J., Guijarro, J.I., Jimenez, J.L., Saibil, H.R., and Dobson, C.M. 2001. Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. J. Mol. Biol. 311: 325-340.
    • (2001) J. Mol. Biol. , vol.311 , pp. 325-340
    • Zurdo, J.1    Guijarro, J.I.2    Jimenez, J.L.3    Saibil, H.R.4    Dobson, C.M.5


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