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Volumn 270, Issue 1, 1997, Pages 89-98

Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature

Author keywords

Folding pathway; Hydrogen exchange; Protein folding; Stability

Indexed keywords

CHYMOTRYPSIN INHIBITOR; GUANIDINE; HYDROGEN; PROTON; SOLVENT;

EID: 0031552590     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1049     Document Type: Article
Times cited : (82)

References (30)
  • 2
    • 0014604482 scopus 로고
    • Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25°C
    • Aune K. C., Tanford C. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25°C. Biochemistry. 8:1969;4586-4590.
    • (1969) Biochemistry , vol.8 , pp. 4586-4590
    • Aune, K.C.1    Tanford, C.2
  • 3
    • 0029865938 scopus 로고    scopus 로고
    • Future directions in protein folding: The multi-state nature of protein structure
    • Bai Y., Englander S. W. Future directions in protein folding: the multi-state nature of protein structure. Proteins: Struct. Funct. Genet. 24:1996;145-151.
    • (1996) Proteins: Struct. Funct. Genet. , vol.24 , pp. 145-151
    • Bai, Y.1    Englander, S.W.2
  • 6
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange intermediates
    • Bai Y., Sosnick T. R., Mayne L., Englander S. W. Protein folding intermediates: native-state hydrogen exchange intermediates. Science. 269:1995;192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 7
    • 0029746061 scopus 로고    scopus 로고
    • Detection of rare partially folded molecules in equilibrium with the native conformations of RNase H
    • Chamberlain A. K., Handel T. M., Marqusee S. Detection of rare partially folded molecules in equilibrium with the native conformations of RNase H. Nature Struct. Biol. 3:1996;782-787.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 782-787
    • Chamberlain, A.K.1    Handel, T.M.2    Marqusee, S.3
  • 8
    • 0030334648 scopus 로고    scopus 로고
    • An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway
    • Clarke J., Fersht A. R. An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Fold. Des. 1:1996;243-254.
    • (1996) Fold. Des. , vol.1 , pp. 243-254
    • Clarke, J.1    Fersht, A.R.2
  • 9
    • 0003932766 scopus 로고
    • New York: W. H. Freeman and Co
    • Creighton T. E. Proteins. 1993;W. H. Freeman and Co, New York.
    • (1993) Proteins
    • Creighton, T.E.1
  • 11
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor-2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki L. S., Otzen D. E., Fersht A. R. The structure of the transition state for folding of chymotrypsin inhibitor-2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254:1995;260-288.
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 12
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor-2. 1. Evidence for a two-state transition
    • Jackson S. E., Fersht A. R. Folding of chymotrypsin inhibitor-2. 1. Evidence for a two-state transition. Biochemistry. 30:1991;10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 13
    • 0027384577 scopus 로고
    • Effect of cavity creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson S. E., Moracci M., elMasry M., Johnson C. M., Fersht A. R. Effect of cavity creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry. 32:1993;11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    ElMasry, M.3    Johnson, C.M.4    Fersht, A.R.5
  • 14
    • 0029061516 scopus 로고
    • Protein stability as a function of denaturant concentration: The thermal stability of barnase in the presence of urea
    • Johnson C. M., Fersht A. R. Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea. Biochemistry. 34:1995;6795-6804.
    • (1995) Biochemistry , vol.34 , pp. 6795-6804
    • Johnson, C.M.1    Fersht, A.R.2
  • 15
    • 0000846433 scopus 로고
    • Sequence specific assignment of the proton nuclear magnetic resonance spectrum of barley serine proteinase inhibitor 2
    • Kjær M., Ludvingsen S., Sorensen O. W., Denys L. A., Kindler J., Poulsen F. M. Sequence specific assignment of the proton nuclear magnetic resonance spectrum of barley serine proteinase inhibitor 2. Carslberg Res. Commun. 52:1987a;353-362.
    • (1987) Carslberg Res. Commun. , vol.52 , pp. 353-362
    • Kjær, M.1    Ludvingsen, S.2    Sorensen, O.W.3    Denys, L.A.4    Kindler, J.5    Poulsen, F.M.6
  • 16
    • 0026346980 scopus 로고
    • Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structure in crystals
    • Ludvigsen S., Shen H., Kjær, M., Madsen J. C., Poulsen F. M. Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structure in crystals. J. Mol. Biol. 222:1991;621-635.
    • (1991) J. Mol. Biol. , vol.222 , pp. 621-635
    • Ludvigsen, S.1    Shen, H.2    Kjær, M.3    Madsen, J.C.4    Poulsen, F.M.5
  • 17
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidinium chloride. A calorimetric study
    • Makhatadze G. I., Privalov P. L. Protein interactions with urea and guanidinium chloride. A calorimetric study. J. Mol. Biol. 226:1992;491-505.
    • (1992) J. Mol. Biol. , vol.226 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 18
    • 0027730340 scopus 로고
    • Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A
    • Mayo S. L., Baldwin R. L. Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A. Science. 262:1993;873-876.
    • (1993) Science , vol.262 , pp. 873-876
    • Mayo, S.L.1    Baldwin, R.L.2
  • 19
    • 0029088938 scopus 로고
    • A statistical mechanical model for hydrogen exchange in globular proteins
    • Miller D. W., Dill K. A. A statistical mechanical model for hydrogen exchange in globular proteins. Protein Sci. 4:1995;1860-1873.
    • (1995) Protein Sci. , vol.4 , pp. 1860-1873
    • Miller, D.W.1    Dill, K.A.2
  • 20
  • 21
    • 0014939368 scopus 로고
    • The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions
    • Nozaki Y., Tanford C. The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions. J. Biol. Chem. 245:1970;1648-1652.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1648-1652
    • Nozaki, Y.1    Tanford, C.2
  • 22
    • 0027948175 scopus 로고
    • Structure of the transition state for the folding/unfolding of chymotrypsin inhibitor-2 and its implications for mechanisms of protein folding
    • Otzen D. E., Itzhaki L. S., elMasry N. F., Jackson S. E., Fersht A. R. Structure of the transition state for the folding/unfolding of chymotrypsin inhibitor-2 and its implications for mechanisms of protein folding. Proc. Natl Acad. Sci. USA. 91:1994;10422-10425.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10422-10425
    • Otzen, D.E.1    Itzhaki, L.S.2    ElMasry, N.F.3    Jackson, S.E.4    Fersht, A.R.5
  • 23
    • 0022555885 scopus 로고
    • Determination and anlysis of urea and guanidine hydrochloride denturation curves
    • Pace C. N. Determination and anlysis of urea and guanidine hydrochloride denturation curves. Methods. Enzymol. 131:1986;266-280.
    • (1986) Methods. Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 24
    • 0029053552 scopus 로고
    • Folding of a nascent polypeptide chain in vitro: Cooperative formation of structure in a protein module
    • Prat Gay G. de, Ruiz-Sanz J., Neira J. L., Itzhaki L. S., Fersht A. R. Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module. Proc. Natl Acad. Sci. USA, 92:1995;3683-3686.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3683-3686
    • Prat De Gay, G.1    Ruiz-Sanz, J.2    Neira, J.L.3    Itzhaki, L.S.4    Fersht, A.R.5
  • 25
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov P. L., Potemkhin S. A. Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods. Enzymol. 131:1986;4-51.
    • (1986) Methods. Enzymol. , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potemkhin, S.A.2
  • 26
    • 0027977883 scopus 로고
    • Protein hydrogen exchange in denaturant: Quantitative analysis by a two process model
    • Qian H., Mayo S. L., Morton A. Protein hydrogen exchange in denaturant: quantitative analysis by a two process model. Biochemistry. 33:1994;8167-8171.
    • (1994) Biochemistry , vol.33 , pp. 8167-8171
    • Qian, H.1    Mayo, S.L.2    Morton, A.3
  • 27
    • 0024375552 scopus 로고
    • Effects of denaturants at low concentrations on the reversible denaturation of staphylococcal nuclease
    • Shortle D., Meeker A. K., Freire E. Effects of denaturants at low concentrations on the reversible denaturation of staphylococcal nuclease. Arch. Biochem. Biophys. 272:1989;103-113.
    • (1989) Arch. Biochem. Biophys. , vol.272 , pp. 103-113
    • Shortle, D.1    Meeker, A.K.2    Freire, E.3
  • 28
    • 0027432960 scopus 로고
    • Low energy activation for amide hydrogen exchange reactions in proteins supports a local unfolding model
    • Thomsen N. K., Poulsen F. M. Low energy activation for amide hydrogen exchange reactions in proteins supports a local unfolding model. J. Mol. Biol. 234:1993;234-241.
    • (1993) J. Mol. Biol. , vol.234 , pp. 234-241
    • Thomsen, N.K.1    Poulsen, F.M.2
  • 29
    • 0018368695 scopus 로고
    • Hydrogen exchange kinetics and internal motions in proteins and nucleic acids
    • Woodward C. K., Hilton B. D. Hydrogen exchange kinetics and internal motions in proteins and nucleic acids. Annu. Rev. Biophys. Bioeng. 8:1979;99-127.
    • (1979) Annu. Rev. Biophys. Bioeng. , vol.8 , pp. 99-127
    • Woodward, C.K.1    Hilton, B.D.2
  • 30
    • 0019076960 scopus 로고
    • Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor
    • Woodward C. K., Hilton B. D. Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor. Biophys. J. 32:1980;561-575.
    • (1980) Biophys. J. , vol.32 , pp. 561-575
    • Woodward, C.K.1    Hilton, B.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.