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Volumn 75, Issue 1, 1998, Pages 445-452

High-resolution, high-pressure NMR studies of proteins

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME; RIBONUCLEASE A; UBIQUITIN;

EID: 0031836878     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77532-0     Document Type: Article
Times cited : (64)

References (35)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C. B. 1973. Principles that govern the folding of protein chains. Science. 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 0002450495 scopus 로고    scopus 로고
    • High-resolution NMR probe for experiments at high pressures
    • Ballard, L., C. Reiner, and J. Jonas. 1996. High-resolution NMR probe for experiments at high pressures. J. Magn. Res. 123A:81-86.
    • (1996) J. Magn. Res. , vol.123 A , pp. 81-86
    • Ballard, L.1    Reiner, C.2    Jonas, J.3
  • 4
    • 0032113596 scopus 로고    scopus 로고
    • A high pressure, high resolution NMR probe for experiments at 500 MHz
    • in press
    • Ballard, L., A. Yu, C. Reiner, and J. Jonas. 1998. A high pressure, high resolution NMR probe for experiments at 500 MHz. J. Magn. Res. (in press).
    • (1998) J. Magn. Res.
    • Ballard, L.1    Yu, A.2    Reiner, C.3    Jonas, J.4
  • 5
    • 0026607096 scopus 로고
    • Early hydrogen-bonding events in the folding reaction of ubiquitin
    • Briggs, M. S., and H. Roder. 1992. Early hydrogen-bonding events in the folding reaction of ubiquitin. Proc. Natl. Acad. Sci. USA. 89:2017-2021.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2017-2021
    • Briggs, M.S.1    Roder, H.2
  • 6
    • 0028349704 scopus 로고
    • Amide hydrogen exchange in a highly denatured state: Hen egg-white lysozyrne in urea
    • Buck, M., S. E. Radford, and C. M. Dobson. 1994. Amide hydrogen exchange in a highly denatured state: hen egg-white lysozyrne in urea. J. Mol. Biol. 237:247-254.
    • (1994) J. Mol. Biol. , vol.237 , pp. 247-254
    • Buck, M.1    Radford, S.E.2    Dobson, C.M.3
  • 7
    • 0017801999 scopus 로고
    • Pressure effects on folded proteins in solution
    • Carter, J. V., D. G. Knox, and A. Rosenberg. 1978. Pressure effects on folded proteins in solution. J. Biol. Chem. 253:1947-1953.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1947-1953
    • Carter, J.V.1    Knox, D.G.2    Rosenberg, A.3
  • 8
  • 9
    • 0023522384 scopus 로고
    • 1H NMR study of human ubiquitin: A main chain directed assignment and structure analysis
    • 1H NMR study of human ubiquitin: a main chain directed assignment and structure analysis. Biochemistry. 26:7272-7281.
    • (1987) Biochemistry , vol.26 , pp. 7272-7281
    • Di Stefano, D.L.1    Wand, A.J.2
  • 10
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink, A. L. 1995. Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct 24:495-522.
    • (1995) Annu. Rev. Biophys. Biomol. Struct , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 11
    • 0030322627 scopus 로고    scopus 로고
    • Structure of very early protein folding intermediates: New insights through a variant of hydrogen exchange labeling
    • Gladwin, S. T., and P. A. Evans. 1996. Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labeling. Folding Des. 1:407-417.
    • (1996) Folding Des. , vol.1 , pp. 407-417
    • Gladwin, S.T.1    Evans, P.A.2
  • 12
    • 0025731274 scopus 로고
    • Characterization of a partially denatured state of a protein by two-dimensional NMR: Reduction of the hydrophobic interactions in ubiquitin
    • Harding, M. H., D. H. Williams, and D. N. Woolfson. 1991. Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin. Biochemistry. 30:3120-3128.
    • (1991) Biochemistry , vol.30 , pp. 3120-3128
    • Harding, M.H.1    Williams, D.H.2    Woolfson, D.N.3
  • 13
    • 0029811091 scopus 로고    scopus 로고
    • Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchange
    • Houry, W. A., and H. A. Scheraga. 1996. Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchange. Biochemistry. 35:11734-11746.
    • (1996) Biochemistry , vol.35 , pp. 11734-11746
    • Houry, W.A.1    Scheraga, H.A.2
  • 14
    • 0029934661 scopus 로고    scopus 로고
    • Heat and cold denatured states of monomeric λ repressor are thermodynamically and conformationally equivalent
    • Huang, G. S., and T. G. Oas. 1996. Heat and cold denatured states of monomeric λ repressor are thermodynamically and conformationally equivalent. Biochemistry. 35:6173-6180.
    • (1996) Biochemistry , vol.35 , pp. 6173-6180
    • Huang, G.S.1    Oas, T.G.2
  • 15
    • 0000530660 scopus 로고
    • Nuclear magnetic resonance at high pressure
    • Jonas, J. 1982. Nuclear magnetic resonance at high pressure. Science. 216:1179-1184.
    • (1982) Science , vol.216 , pp. 1179-1184
    • Jonas, J.1
  • 16
    • 0028226052 scopus 로고
    • High-pressure NMR spectroscopy of proteins and membranes
    • Jonas, J., and A. 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, J.1    Jonas, A.2
  • 18
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh, S., I. D. Peters, and H. Roder. 1996. Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nature Struct. Biol. 3:193-205.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 19
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P. S., and R. L. Baldwin. 1990. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 20
    • 0029126840 scopus 로고
    • Solution x-ray scattering analysis of cold-, heat-, and urea-denatured states in a protein, Streptomyces subtilisin inhibitor
    • Konno, T., M. Kataoka, Y. Kamatari, K. Kanaori, A. Nosaka, and K. Akasaka. 1995. Solution x-ray scattering analysis of cold-, heat-, and urea-denatured states in a protein, Streptomyces subtilisin inhibitor. J. Mol. Biol. 251:95-103.
    • (1995) J. Mol. Biol. , vol.251 , pp. 95-103
    • Konno, T.1    Kataoka, M.2    Kamatari, Y.3    Kanaori, K.4    Nosaka, A.5    Akasaka, K.6
  • 21
    • 0029813888 scopus 로고    scopus 로고
    • Determination of the activation volume of the uncatalyzed hydrogen exchange reaction between n-methylacetamide and water
    • Mabry, S. A., B.-S. Lee, T. Zheng, and J. Jonas. 1996. Determination of the activation volume of the uncatalyzed hydrogen exchange reaction between n-methylacetamide and water. J. Am. Chem. Soc. 118:8887-8890.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8887-8890
    • Mabry, S.A.1    Lee, B.-S.2    Zheng, T.3    Jonas, J.4
  • 22
    • 0026013162 scopus 로고
    • Demonstration by NMR of folding domains in lysozyme
    • Miranker, A., S. E. Radford, M. Karplus, and C. M. Dobson. 1991. Demonstration by NMR of folding domains in lysozyme. Nature. 349: 633-636.
    • (1991) Nature , vol.349 , pp. 633-636
    • Miranker, A.1    Radford, S.E.2    Karplus, M.3    Dobson, C.M.4
  • 23
    • 0030664959 scopus 로고    scopus 로고
    • Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates
    • Nash, D., and J. Jonas. 1997a. Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates. Biochemistry. 36:14375-14383.
    • (1997) Biochemistry , vol.36 , pp. 14375-14383
    • Nash, D.1    Jonas, J.2
  • 24
    • 0031577539 scopus 로고    scopus 로고
    • Structure of the pressure-assisted cold denatured state of ubiquitin
    • Nash, D., and J. Jonas. 1997b. Structure of the pressure-assisted cold denatured state of ubiquitin. Biochem. Biophys. Res. Commun. 238: 289-291.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 289-291
    • Nash, D.1    Jonas, J.2
  • 25
    • 0030582432 scopus 로고    scopus 로고
    • Hydrogen-exchange kinetics in the cold denatured state of ribonuclease A
    • Nash, D., B.-S. Lee, and J. Jonas. 1996. Hydrogen-exchange kinetics in the cold denatured state of ribonuclease A. Biochim. Biophys. Acta. 1297: 40-48.
    • (1996) Biochim. Biophys. Acta , vol.1297 , pp. 40-48
    • Nash, D.1    Lee, B.-S.2    Jonas, J.3
  • 26
    • 0026460815 scopus 로고
    • Hydrogen exchange in native and alcohol forms of ubiquitin
    • Pan, Y., and M. S. Briggs. 1992. Hydrogen exchange in native and alcohol forms of ubiquitin. Biochemistry. 31:11405-11412.
    • (1992) Biochemistry , vol.31 , pp. 11405-11412
    • Pan, Y.1    Briggs, M.S.2
  • 27
    • 0028917296 scopus 로고
    • Structures of folding intermediates
    • Ptitsyn, O. B. 1995. Structures of folding intermediates. Curr. Opin. Struct. Biol. 5:74-78.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 74-78
    • Ptitsyn, O.B.1
  • 28
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S. E., C. M. Dobson, and P. A. Evans. 1992. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 29
    • 0024284779 scopus 로고
    • 1H NMR assignments and secondary structure of hen egg white lysozyme in solution
    • 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry. 27:122-136.
    • (1988) Biochemistry , vol.27 , pp. 122-136
    • Redfield, C.1    Dobson, C.M.2
  • 31
    • 0025999787 scopus 로고
    • Hydrogen exchange in thermally denatured ribonuclease A
    • Robertson, A. D., and R. L. Baldwin. 1991. Hydrogen exchange in thermally denatured ribonuclease A. Biochemistry. 30:9907-9914.
    • (1991) Biochemistry , vol.30 , pp. 9907-9914
    • Robertson, A.D.1    Baldwin, R.L.2
  • 32
  • 33
    • 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
  • 35
    • 0029040518 scopus 로고
    • NMR study of the cold, heat, and pressure unfolding of ribonuclease A
    • Zhang, J., X. Peng, A. Jonas, and J. Jonas. 1995. NMR study of the cold, heat, and pressure unfolding of ribonuclease A. Biochemistry. 34: 8631-8641.
    • (1995) Biochemistry , vol.34 , pp. 8631-8641
    • Zhang, J.1    Peng, X.2    Jonas, A.3    Jonas, J.4


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