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Volumn 284, Issue 5, 1998, Pages 1625-1639

Characterisation of low free-energy excited states of folded proteins

Author keywords

Excited states; NMR; Protein dynamics; Protein structure; Protein unfolding

Indexed keywords

APROTININ; LYSOZYME; PHOSPHOGLYCERATE KINASE;

EID: 0032545169     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2265     Document Type: Article
Times cited : (74)

References (47)
  • 1
    • 0030858227 scopus 로고    scopus 로고
    • Extracting information from the temperature gradients of polypeptide NH chemical shifts. 1. The importance of conformational averaging
    • Andersen, N. H., Neidigh, J. W., Harris, S. M., Lee, G. M., Liu, Z. & Tong, H. (1997). Extracting information from the temperature gradients of polypeptide NH chemical shifts. 1. The importance of conformational averaging. J. Am. Chem. Soc. 119, 8547-8561.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8547-8561
    • Andersen, N.H.1    Neidigh, J.W.2    Harris, S.M.3    Lee, G.M.4    Liu, Z.5    Tong, H.6
  • 3
    • 0000635348 scopus 로고
    • The relationship between amide proton chemical shifts and secondary structure in proteins
    • Asakura, T., Taoka, K., Demura, M. & Williamson, M. P. (1995). The relationship between amide proton chemical shifts and secondary structure in proteins. J. Biomol. NMR, 6, 227-236.
    • (1995) J. Biomol. NMR , vol.6 , pp. 227-236
    • Asakura, T.1    Taoka, K.2    Demura, M.3    Williamson, M.P.4
  • 4
    • 0029865938 scopus 로고    scopus 로고
    • Future directions in folding: The multi-state nature of protein structure
    • Bai, Y. & Englander, S. W. (1996). Future directions in folding: The multi-state nature of protein structure. Proteins: Struct. Funct. Genet. 24, 145-151.
    • (1996) Proteins: Struct. Funct. Genet. , vol.24 , pp. 145-151
    • Bai, Y.1    Englander, S.W.2
  • 5
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., Sosnick, T. R., Mayne, L. & Englander, S. W. (1995). Protein folding intermediates: native-state hydrogen exchange. Science, 269, 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 7
    • 0026795399 scopus 로고
    • Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures
    • Berndt, K. D., Güntert, P., Orbons, L. P. M. & Wüthrich, K. (1992). Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J. Mol. Biol. 227, 757-775.
    • (1992) J. Mol. Biol. , vol.227 , pp. 757-775
    • Berndt, K.D.1    Güntert, P.2    Orbons, L.P.M.3    Wüthrich, K.4
  • 9
    • 0029746061 scopus 로고    scopus 로고
    • Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
    • Chamberlain, A. K., Handel, T. M. & Marqusee, S. (1996). Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nature Struct. Biol. 3, 782-787.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 782-787
    • Chamberlain, A.K.1    Handel, T.M.2    Marqusee, S.3
  • 10
    • 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. (1996). An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Folding Des. 1, 243-254.
    • (1996) Folding Des. , vol.1 , pp. 243-254
    • Clarke, J.1    Fersht, A.R.2
  • 11
    • 0031205431 scopus 로고    scopus 로고
    • Protein folding pathways and intermediates
    • Clarke, A. R. & Waltho, J. P. (1997). Protein folding pathways and intermediates. Curr. Opin. Biotechnol. 8, 400-410.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 400-410
    • Clarke, A.R.1    Waltho, J.P.2
  • 13
  • 15
    • 0029994817 scopus 로고    scopus 로고
    • Using buried water molecules to explore the energy landscape of proteins
    • Denisov, V. A., Peters, J., Hörlein, H. D. & Halle, B. (1996). Using buried water molecules to explore the energy landscape of proteins. Nature Struct. Biol. 3, 505-509.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 505-509
    • Denisov, V.A.1    Peters, J.2    Hörlein, H.D.3    Halle, B.4
  • 16
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A. & Chan, H. S. (1997). From Levinthal to pathways to funnels. Nature Struct. Biol. 4, 10-19.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 17
    • 0024278597 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. 1. Sequence requirements for the formation of a reverse turn
    • Dyson, H. J., Rance, M., Houghten, R. A., Lerner, R. A. & Wright, P. E. (1988). Folding of immunogenic peptide fragments of proteins in water solution. 1. Sequence requirements for the formation of a reverse turn. J. Mol. Biol. 201, 161-200.
    • (1988) J. Mol. Biol. , vol.201 , pp. 161-200
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Lerner, R.A.4    Wright, P.E.5
  • 19
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., Sligar, S. G. & Wolynes, P. G. (1991). The energy landscapes and motions of proteins. Science, 254, 1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 21
    • 0031019315 scopus 로고    scopus 로고
    • Is the structure of the N-domain of phosphoglycerate kinase affected by isolation from the intact molecule?
    • Hosszu, L. L. P., Craven, C. J., Spencer, J., Parker, M. J., Clarke, A. R., Kelly, M. & Waltho, J. P. (1997b). Is the structure of the N-domain of phosphoglycerate kinase affected by isolation from the intact molecule? Biochemistry, 36, 333-340.
    • (1997) Biochemistry , vol.36 , pp. 333-340
    • Hosszu, L.L.P.1    Craven, C.J.2    Spencer, J.3    Parker, M.J.4    Clarke, A.R.5    Kelly, M.6    Waltho, J.P.7
  • 22
    • 0031552590 scopus 로고    scopus 로고
    • Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature
    • Itzhaki, L. S., Neira, J. L. & Fersht, A. R. (1997). Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature. J. Mol. Biol. 270, 89-98.
    • (1997) J. Mol. Biol. , vol.270 , pp. 89-98
    • Itzhaki, L.S.1    Neira, J.L.2    Fersht, A.R.3
  • 23
    • 0026645602 scopus 로고
    • Variability of conformations at crystal contacts in BPTI represent true low-energy structures: Correspondence among lattice packing and molecular dynamics structures
    • Kossiakoff, A. A., Randal, M., Guenot, J. & Eigenbrot, C. (1992). Variability of conformations at crystal contacts in BPTI represent true low-energy structures: correspondence among lattice packing and molecular dynamics structures. Proteins: Struct. Funct. Genet. 14, 65-74.
    • (1992) Proteins: Struct. Funct. Genet. , vol.14 , pp. 65-74
    • Kossiakoff, A.A.1    Randal, M.2    Guenot, J.3    Eigenbrot, C.4
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 25
    • 0029140564 scopus 로고
    • The influence of temperature on lysozyme crystals: Structure and dynamics of protein and water
    • Kurinov, I. V. & Harrison, R. W. (1995). The influence of temperature on lysozyme crystals: structure and dynamics of protein and water. Acta Crystallog. sect. D, 51, 98-109.
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 98-109
    • Kurinov, I.V.1    Harrison, R.W.2
  • 26
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. & Richards, F. M. (1971). The interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol. 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 27
    • 0029283884 scopus 로고
    • Chemical shifts and 3-dimensional protein structures
    • Oldfield, E. (1995). Chemical shifts and 3-dimensional protein structures. J. Biomol. NMR, 5, 217-225.
    • (1995) J. Biomol. NMR , vol.5 , pp. 217-225
    • Oldfield, E.1
  • 28
    • 0000865993 scopus 로고
    • A new analysis of proton chemical shifts in proteins
    • Ösapay, K. & Case, D. A. (1991). A new analysis of proton chemical shifts in proteins. J. Am. Chem. Soc. 113, 9436-9444.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9436-9444
    • Ösapay, K.1    Case, D.A.2
  • 29
    • 0027155345 scopus 로고
    • Disulfide bond isomerization in BPTI and BPTI(G36S); an NMR study of correlated mobility in proteins
    • Otting, G., Liepinsh, E. & Wüthrich, K. (1993). Disulfide bond isomerization in BPTI and BPTI(G36S); an NMR study of correlated mobility in proteins. Biochemistry, 2, 3571-3582.
    • (1993) Biochemistry , vol.2 , pp. 3571-3582
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 30
    • 0028791393 scopus 로고
    • An integrated kinetic analysis of intermediates and transition states in protein folding reactions
    • Parker, M. J., Spencer, J. & Clarke, A. R. (1995). An integrated kinetic analysis of intermediates and transition states in protein folding reactions. J. Mol. Biol. 253, 771-786.
    • (1995) J. Mol. Biol. , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clarke, A.R.3
  • 33
    • 0018588511 scopus 로고
    • Stability of proteins
    • Privalov, P. L. (1979). Stability of proteins. Advan. Protein Chem. 33, 167-241.
    • (1979) Advan. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 34
    • 0024209251 scopus 로고
    • Secondary structure of the Arg-Gly-Asp recognition site in proteins involved in cell-surface adhesion
    • Reed, J., Hull, W. E., von der Lieth, C.-W., Kübler, D., Suhai, S. & Kinzel, V. (1988). Secondary structure of the Arg-Gly-Asp recognition site in proteins involved in cell-surface adhesion. Eur. J. Biochem. 178, 141-154.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 141-154
    • Reed, J.1    Hull, W.E.2    Von Der Lieth, C.-W.3    Kübler, D.4    Suhai, S.5    Kinzel, V.6
  • 35
    • 0027981211 scopus 로고
    • Structure and dynamics of the neutrophil defensins NP-2, NP-5, and NP-1: NMR studies of amide hydrogen exchange kinetics
    • Skalicky, J. J., Selsted, M. E. & Pardi, A. (1994). Structure and dynamics of the neutrophil defensins NP-2, NP-5, and NP-1: NMR studies of amide hydrogen exchange kinetics. Proteins: Struct. Funct. Genet. 20, 52-67.
    • (1994) Proteins: Struct. Funct. Genet. , vol.20 , pp. 52-67
    • Skalicky, J.J.1    Selsted, M.E.2    Pardi, A.3
  • 38
    • 0026606219 scopus 로고
    • Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 K to 320 K
    • Tilton, R. F., Dewan, J. C. & Petsko, G. A. (1992). Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 K to 320 K. Biochemistry, 31, 2469-2481.
    • (1992) Biochemistry , vol.31 , pp. 2469-2481
    • Tilton, R.F.1    Dewan, J.C.2    Petsko, G.A.3
  • 39
    • 0022211670 scopus 로고
    • Hydrogen exchange kinetics of amide protons at the bovine pancreatic trypsin inhibitor protein-solvent interface
    • Tüchsen, E. & Woodward, C. (1985). Hydrogen exchange kinetics of amide protons at the bovine pancreatic trypsin inhibitor protein-solvent interface. J. Mol. Biol. 185, 405-419.
    • (1985) J. Mol. Biol. , vol.185 , pp. 405-419
    • Tüchsen, E.1    Woodward, C.2
  • 40
    • 0023660041 scopus 로고
    • Hydrogen exchange kinetics of surface peptide amides in bovine pancreatic trypsin inhibitor
    • Tüchsen, E. & Woodward, C. (1987). Hydrogen exchange kinetics of surface peptide amides in bovine pancreatic trypsin inhibitor. J. Mol. Biol. 193, 793-802.
    • (1987) J. Mol. Biol. , vol.193 , pp. 793-802
    • Tüchsen, E.1    Woodward, C.2
  • 41
    • 0020483829 scopus 로고
    • Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution
    • Wagner, G. & Wüthrich, K. (1982). Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. J. Mol. Biol. 160, 343-361.
    • (1982) J. Mol. Biol. , vol.160 , pp. 343-361
    • Wagner, G.1    Wüthrich, K.2
  • 43
    • 44949269218 scopus 로고
    • Empirical comparisons of models for chemical shift calculation in proteins
    • Williamson, M. P. & Asakura, T. (1993). Empirical comparisons of models for chemical shift calculation in proteins. J. Magn. Reson. 101B, 63-71.
    • (1993) J. Magn. Reson. , vol.101 B , pp. 63-71
    • Williamson, M.P.1    Asakura, T.2
  • 44
    • 0021603710 scopus 로고
    • Structure of bovine pancreatic trypsin inhibitor: Results of joint neutron and X-ray refinement of crystal form II
    • Wlodawer, A., Walter, J., Huber, R. & Sjolin, L. (1984). Structure of bovine pancreatic trypsin inhibitor: Results of joint neutron and X-ray refinement of crystal form II. J. Mol. Biol. 180, 301-329.
    • (1984) J. Mol. Biol. , vol.180 , pp. 301-329
    • Wlodawer, A.1    Walter, J.2    Huber, R.3    Sjolin, L.4
  • 45
    • 0029109378 scopus 로고
    • NMR: This other method for protein and nucleic acid structure determination
    • Wüthrich, K. (1995). NMR: This other method for protein and nucleic acid structure determination. Acta Crystallog. sect. D, 51, 249-270.
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 249-270
    • Wüthrich, K.1
  • 46
    • 0018782084 scopus 로고
    • Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor
    • Wüthrich, K. & Wagner, G. (1979). Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor. J. Mol. Biol. 130, 1-18.
    • (1979) J. Mol. Biol. , vol.130 , pp. 1-18
    • Wüthrich, K.1    Wagner, G.2
  • 47
    • 0028013478 scopus 로고
    • Thermal expansion of hen egg-white lysozyme: Comparison of the 1.9 Å resolution structures of the tetragonal form of the enzyme at 100 K and 298 K
    • Young, A. C. M., Tilton, R. F. & Dewan, J. C. (1994). Thermal expansion of hen egg-white lysozyme: Comparison of the 1.9 Å resolution structures of the tetragonal form of the enzyme at 100 K and 298 K. J. Mol. Biol. 235, 302-317.
    • (1994) J. Mol. Biol. , vol.235 , pp. 302-317
    • Young, A.C.M.1    Tilton, R.F.2    Dewan, J.C.3


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