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Volumn 83, Issue 4, 2002, Pages 2259-2269

Pretransitional structural changes in the thermal denaturation of ribonuclease S and S protein

Author keywords

[No Author keywords available]

Indexed keywords

RIBONUCLEASE; RIBONUCLEASE A; RIBONUCLEASE S; UNCLASSIFIED DRUG; VITRONECTIN;

EID: 0036789422     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)73986-6     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 0034630136 scopus 로고    scopus 로고
    • Enhanced prediction accuracy of protein secondary structure using hydrogen exchange FT-IR spectroscopy
    • Baello, B. I., P. Pancoska, and T. A. Keiderling. 2000. Enhanced prediction accuracy of protein secondary structure using hydrogen exchange FT-IR spectroscopy. Anal. Biochem. 280:46-57.
    • (2000) Anal. Biochem. , vol.280 , pp. 46-57
    • Baello, B.I.1    Pancoska, P.2    Keiderling, T.A.3
  • 3
    • 0029797086 scopus 로고    scopus 로고
    • Temperature-induced denaturation of ribonuclease S: A thermodynamic study
    • Catazano, F., C. Giancola, G. Graziano, and G. Barone. 1996. Temperature-induced denaturation of ribonuclease S: a thermodynamic study. Biochemistry. 35:13378-13385.
    • (1996) Biochemistry , vol.35 , pp. 13378-13385
    • Catazano, F.1    Giancola, C.2    Graziano, G.3    Barone, G.4
  • 4
    • 0033529212 scopus 로고    scopus 로고
    • Native-state hydrogen-exchange studies of a fragment complex can provide structural information about the isolated fragments
    • Chakshusmati, G., G. S. Ratnaparkhi, P. K. Madhu, and R. Varadarajan. 1999. Native-state hydrogen-exchange studies of a fragment complex can provide structural information about the isolated fragments. Proc. Natl. Acad. Sci. U. S. A. 96:7899-7904.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 7899-7904
    • Chakshusmati, G.1    Ratnaparkhi, G.S.2    Madhu, P.K.3    Varadarajan, R.4
  • 5
    • 0001196094 scopus 로고    scopus 로고
    • Study of the ribonuclease S-peptide/S-protein complex by means of Raman difference spectroscopy
    • Gilmanshin. R., J. Van Beek, and R. H. Callender. 1996. Study of the ribonuclease S-peptide/S-protein complex by means of Raman difference spectroscopy. J. Phys. Chem. 100:16755-16760
    • (1996) J. Phys. Chem. , vol.100 , pp. 16755-16760
    • Gilmanshin, R.1    Van Beek, J.2    Callender, R.H.3
  • 6
    • 0032562222 scopus 로고    scopus 로고
    • Kinetic mechanism of a partial folding reaction: 2. Nature of the transition state
    • Goldberg, J. M., and R. L. Baldwin. 1998. Kinetic mechanism of a partial folding reaction: 2. Nature of the transition state. Biochemistry. 37: 2556-2563.
    • (1998) Biochemistry , vol.37 , pp. 2556-2563
    • Goldberg, J.M.1    Baldwin, R.L.2
  • 8
    • 0000291490 scopus 로고
    • Chiroptical properties of proteins: 1. Near-ultraviolet circular dichroism of ribonuclease S
    • Goux, W. J., and T. M. J. Hooker. 1980. Chiroptical properties of proteins: 1. Near-ultraviolet circular dichroism of ribonuclease S. J. Am. Chem. Soc. 102:7080-7087.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7080-7087
    • Goux, W.J.1    Hooker, T.M.J.2
  • 9
    • 0029826093 scopus 로고    scopus 로고
    • DSC study of the thermal stability of S-protein and S-peptide/S-protein complexes
    • Graziano, G., F. Catazano, C. Giancola, and G. Barone. 1996. DSC study of the thermal stability of S-protein and S-peptide/S-protein complexes. Biochemistry. 35:13386-13392.
    • (1996) Biochemistry , vol.35 , pp. 13386-13392
    • Graziano, G.1    Catazano, F.2    Giancola, C.3    Barone, G.4
  • 10
    • 0023047824 scopus 로고
    • A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease S
    • Haris, P. I., D. C. Lee, and D. Chapman. 1986. A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease S. Biochim. Biophys. Acta. 874:2:55-265.
    • (1986) Biochim. Biophys. Acta , vol.874 , pp. 255-265
    • Haris, P.I.1    Lee, D.C.2    Chapman, D.3
  • 11
    • 0015207678 scopus 로고
    • Thermodynamics of the binding of S-peptide to S-protein to form ribonuclease S'
    • Hearn, R. P., F. M. Richards, J. M. Sturtevant, and G. D. Watt. 1971. Thermodynamics of the binding of S-peptide to S-protein to form ribonuclease S'. Biochemistry. 10:806-817.
    • (1971) Biochemistry , vol.10 , pp. 806-817
    • Hearn, R.P.1    Richards, F.M.2    Sturtevant, J.M.3    Watt, G.D.4
  • 12
    • 0015217923 scopus 로고
    • Absorption and circular dichroism spectra of ribonuclease-S at 77°K
    • Horwitz, J., and E. H. Strickland. 1971. Absorption and circular dichroism spectra of ribonuclease-S at 77°K. J. Biol. Chem. 246:3749-3752.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3749-3752
    • Horwitz, J.1    Strickland, E.H.2
  • 13
    • 0000042757 scopus 로고    scopus 로고
    • Peptide and protein conformational studies with vibrational circular dichroism and related spectroscopies
    • N. Berova, K. Nakanishi, and R. W. Woody, editors. Wiley, New York
    • Keiderling, T. A. 2000. Peptide and protein conformational studies with vibrational circular dichroism and related spectroscopies. In Circular Dichroism: Principles and Applications. N. Berova, K. Nakanishi, and R. W. Woody, editors. Wiley, New York. 621-666.
    • (2000) Circular Dichroism: Principles and Applications , pp. 621-666
    • Keiderling, T.A.1
  • 14
    • 0026999215 scopus 로고
    • Refinement of the crystal structure of ribonuclease S: Comparison with and between the various ribonuclease A structures
    • Kim, E. E., R. Vadarajan, H. W. Wyckoff, and F. M Richards. 1992. Refinement of the crystal structure of ribonuclease S: comparison with and between the various ribonuclease A structures. Biochemistry. 31: 12304-12314.
    • (1992) Biochemistry , vol.31 , pp. 12304-12314
    • Kim, E.E.1    Vadarajan, R.2    Wyckoff, H.W.3    Richards, F.M.4
  • 15
    • 0014315489 scopus 로고
    • Studies of the conformation of ribonuclease S-peptide
    • Klee, W. A. 1968. Studies of the conformation of ribonuclease S-peptide. Biochemistry. 8:2731-2736.
    • (1968) Biochemistry , vol.8 , pp. 2731-2736
    • Klee, W.A.1
  • 17
    • 0019944760 scopus 로고
    • Secondary structure in ribonuclease: I. Equilibrium folding transitions seen by amide circular dichroism
    • Labhardt, A. 1982. Secondary structure in ribonuclease: I. Equilibrium folding transitions seen by amide circular dichroism. J. Mol. Biol. 157:331-355.
    • (1982) J. Mol. Biol. , vol.157 , pp. 331-355
    • Labhardt, A.1
  • 18
    • 84985698770 scopus 로고
    • An equilibrium folding intermediate detected in the thermal unfolding of ribonuclease S by circular dichroism
    • Labhardt, A. M. 1981. An equilibrium folding intermediate detected in the thermal unfolding of ribonuclease S by circular dichroism. Biopolymers. 20:1450-1480.
    • (1981) Biopolymers , vol.20 , pp. 1450-1480
    • Labhardt, A.M.1
  • 19
    • 0018801514 scopus 로고
    • Recombination of S-peptide with S-protein during folding of ribonuclease S: I. Folding pathways of the slow-folding and fast-folding classes of unfolded S-protein
    • Labhardt, A. M., and R. L. Baldwin. 1979. Recombination of S-peptide with S-protein during folding of ribonuclease S: I. Folding pathways of the slow-folding and fast-folding classes of unfolded S-protein. J. Mol. Biol. 135:231-244.
    • (1979) J. Mol. Biol. , vol.135 , pp. 231-244
    • Labhardt, A.M.1    Baldwin, R.L.2
  • 20
    • 0013943915 scopus 로고
    • Validity of the "two-state" hypothesis for conformational transitions of proteins
    • Lumry, R., R. Biltonen, and J. Brandts. 1966. Validity of the "two-state" hypothesis for conformational transitions of proteins. Biopolymers. 4:917-944.
    • (1966) Biopolymers , vol.4 , pp. 917-944
    • Lumry, R.1    Biltonen, R.2    Brandts, J.3
  • 23
    • 0028700493 scopus 로고
    • Quantitative analysis of vibrational circular dichroism spectra of proteins: Problems and perspectives
    • Pancoska, P., E. Bitto, V. Janota, and T. A. Keiderling. 1994. Quantitative analysis of vibrational circular dichroism spectra of proteins: problems and perspectives. Faraday Discuss. 99:287-310.
    • (1994) Faraday Discuss , vol.99 , pp. 287-310
    • Pancoska, P.1    Bitto, E.2    Janota, V.3    Keiderling, T.A.4
  • 24
    • 0029011672 scopus 로고
    • Comparison of and limits of accuracy for statistical analyses of vibrational and electronic circular dichroism spectra in terms of correlations to and predictions of protein secondary structure
    • Pancoska, P., E. Bitto, V. Janota, M. Urbanova, V. P. Gupta, and T. A. Keiderling. 1995. Comparison of and limits of accuracy for statistical analyses of vibrational and electronic circular dichroism spectra in terms of correlations to and predictions of protein secondary structure. Protein Sci. 4: 1384-1401.
    • (1995) Protein Sci. , vol.4 , pp. 1384-1401
    • Pancoska, P.1    Bitto, E.2    Janota, V.3    Urbanova, M.4    Gupta, V.P.5    Keiderling, T.A.6
  • 25
    • 0025734103 scopus 로고
    • Statistical analysis of the vibrational circular dichroism of selected proteins and relationship to secondary structures
    • Pancoska, P., S. C. Yasui, and T. A. Keiderling. 1991. Statistical analysis of the vibrational circular dichroism of selected proteins and relationship to secondary structures. Biochemistry. 30:5089-5103.
    • (1991) Biochemistry , vol.30 , pp. 5089-5103
    • Pancoska, P.1    Yasui, S.C.2    Keiderling, T.A.3
  • 26
    • 84965093921 scopus 로고
    • The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein components
    • Richards, F. M., and P. J. Vithayathil. 1959. The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein components. J. Biol. Chem. 234:1459-1465.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1459-1465
    • Richards, F.M.1    Vithayathil, P.J.2
  • 29
    • 0017749336 scopus 로고
    • Mechanism of dissociation of S-peptide from ribonuclease S
    • Schreier, A. A., and R. L. Baldwin. 1977. Mechanism of dissociation of S-peptide from ribonuclease S. Biochemistry. 16:4203-4209.
    • (1977) Biochemistry , vol.16 , pp. 4203-4209
    • Schreier, A.A.1    Baldwin, R.L.2
  • 30
    • 49749180154 scopus 로고
    • Some spectrometric and polarimetric experiments with ribonuclease
    • Sela, M., and C. B. Anfinsen. 1957. Some spectrometric and polarimetric experiments with ribonuclease. Biophys. Biochim. Acta. 24:229-235.
    • (1957) Biophys. Biochim. Acta , vol.24 , pp. 229-235
    • Sela, M.1    Anfinsen, C.B.2
  • 31
    • 0028349385 scopus 로고
    • Thermally denatured ribonuclease A retains secondary structure as shown by FTIR
    • Seshadri, S., K. A. Oberg, and A. L. Fink. 1994. Thermally denatured ribonuclease A retains secondary structure as shown by FTIR. Biochemistry. 33:1351-1355.
    • (1994) Biochemistry , vol.33 , pp. 1351-1355
    • Seshadri, S.1    Oberg, K.A.2    Fink, A.L.3
  • 32
    • 0013809399 scopus 로고
    • Conformational studies of pancreatic ribonuclease and its subtilisin-produced derivatives
    • Sherwood, L. M., and J. T. J. Potts. 1965. Conformational studies of pancreatic ribonuclease and its subtilisin-produced derivatives. J. Biol. Chem. 240:3799-3805.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3799-3805
    • Sherwood, L.M.1    Potts, J.T.J.2
  • 33
    • 0018792624 scopus 로고
    • Conformation of ribonuclease S-protein
    • Shindo, H., S. Matsuura, and J. S. Cohen. 1979. Conformation of ribonuclease S-protein. Experientia. 35:1284-1285.
    • (1979) Experientia , vol.35 , pp. 1284-1285
    • Shindo, H.1    Matsuura, S.2    Cohen, J.S.3
  • 34
    • 0014670414 scopus 로고
    • Thermal effects on the circular dichroism spectra of ribonuclease A and of ribonuclease S-protein
    • Simons, E. R., E. G. Schneider, and E. R. Blout. 1969. Thermal effects on the circular dichroism spectra of ribonuclease A and of ribonuclease S-protein. J. Biol. Chem. 244:4023-4026.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4023-4026
    • Simons, E.R.1    Schneider, E.G.2    Blout, E.R.3
  • 35
    • 0026733250 scopus 로고
    • Denatured states of ribonuclease A have compact dimensions and residual secondary structure
    • Sosnick, T. R., and J. Trewhella. 1992. Denatured states of ribonuclease A have compact dimensions and residual secondary structure. Biochemistry. 31:8329-8335.
    • (1992) Biochemistry , vol.31 , pp. 8329-8335
    • Sosnick, T.R.1    Trewhella, J.2
  • 36
    • 0035055977 scopus 로고    scopus 로고
    • Thermal unfolding of ribonuclease A in phosphate at neutral pH: Deviations from the two state model
    • Stelea, S., P. Pancoska, and T. A. Keiderling. 2001. Thermal unfolding of ribonuclease A in phosphate at neutral pH: deviations from the two state model. Protein Sci. 10:970-978.
    • (2001) Protein Sci. , vol.10 , pp. 970-978
    • Stelea, S.1    Pancoska, P.2    Keiderling, T.A.3
  • 37
    • 0015528751 scopus 로고
    • Interactions contributing to the tyrosyl circular dichroism bands of ribonuclease S and A
    • Strickland, E. H. 1972. Interactions contributing to the tyrosyl circular dichroism bands of ribonuclease S and A. Biochemistry. 11:3465-3474.
    • (1972) Biochemistry , vol.11 , pp. 3465-3474
    • Strickland, E.H.1
  • 38
    • 0026998178 scopus 로고
    • Crystallographic structures of ribonuclease S variants with nonpolar substitution at position 13: Packing and cavities
    • Vadarajan, R., and F. M. Richards. 1992. Crystallographic structures of ribonuclease S variants with nonpolar substitution at position 13: packing and cavities. Biochemistry. 31:12315-12327.
    • (1992) Biochemistry , vol.31 , pp. 12315-12327
    • Vadarajan, R.1    Richards, F.M.2
  • 40
    • 0020478577 scopus 로고
    • The refined crystal structure of ribonuclease A at 2.0 A resolution
    • Wlodawer, A., R. Bott, and L. Sjolin. 1982. The refined crystal structure of ribonuclease A at 2.0 A resolution. J. Biol. Chem. 257:1325-1332.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1325-1332
    • Wlodawer, A.1    Bott, R.2    Sjolin, L.3
  • 41
    • 0014961294 scopus 로고
    • The three-dimensional structure of ribonuclease-S: Interpretation of an electron density map at a nominal resolution of 2 A
    • Wyckoff, H. W., D. Tsemoglou, A. W. Hanson, J. R. Knox, B. Lee, and F. M. Richards. 1970. The three-dimensional structure of ribonuclease-S: interpretation of an electron density map at a nominal resolution of 2 A. J. Biol. Chem. 245:305-328.
    • (1970) J. Biol. Chem. , vol.245 , pp. 305-328
    • Wyckoff, H.W.1    Tsemoglou, D.2    Hanson, A.W.3    Knox, J.R.4    Lee, B.5    Richards, F.M.6


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