메뉴 건너뛰기




Volumn 261, Issue 3, 1996, Pages 443-453

Insight into a random coil conformation and an isolated helix: Structural and dynamical characterisation of the C-helix peptide from hen lysozyme

Author keywords

Hydrogen exchange; Nuclear magnetic resonance; Peptide; Protein folding; Random coil

Indexed keywords

LYSOZYME; PEPTIDE; TRIFLUOROETHANOL;

EID: 0030599012     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0475     Document Type: Article
Times cited : (45)

References (59)
  • 1
    • 0028806684 scopus 로고
    • A comparison of the pH, urea and temperature-denatured states of barnase by heteronuclear NMR: Implications for the initiation of protein folding
    • Arcus, V. L., Vuilleumier, S., Freund, S. M. V., Bycroft, M. & Fersht, A. R. (1995). A comparison of the pH, urea and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding. J. Mol. Biol. 254, 305-321.
    • (1995) J. Mol. Biol. , vol.254 , pp. 305-321
    • Arcus, V.L.1    Vuilleumier, S.2    Freund, S.M.V.3    Bycroft, M.4    Fersht, A.R.5
  • 2
    • 0006393051 scopus 로고
    • Two-dimensional spectroscopy. Applications to nuclear magnetic resonance
    • Aue, W. P., Bartholdi, E. & Ernst, R. R. (1976). Two-dimensional spectroscopy. Applications to nuclear magnetic resonance. J. Chem. Phys. 64, 2229-2246.
    • (1976) J. Chem. Phys. , vol.64 , pp. 2229-2246
    • Aue, W.P.1    Bartholdi, E.2    Ernst, R.R.3
  • 4
    • 0029028490 scopus 로고
    • α-Helix formation by peptides of defined sequence
    • Baldwin, R. L. (1995). α-Helix formation by peptides of defined sequence. Biophys. Chem. 55, 127-135.
    • (1995) Biophys. Chem. , vol.55 , pp. 127-135
    • Baldwin, R.L.1
  • 5
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D. J. & Thornton, J. M. (1988). Helix geometry in proteins. J. Mol. Biol. 201, 601-619.
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 6
    • 0029149907 scopus 로고
    • Protein secondary structure prediction
    • Barton, G. J. (1995). Protein secondary structure prediction. Curr. Opin. Struct. Biol. 5, 372-376.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 372-376
    • Barton, G.J.1
  • 7
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native β-hairpin in aqueous solution
    • Blanco, F. J., Rivas, G. & Serrano, L. (1994). A short linear peptide that folds into a native β-hairpin in aqueous solution. Nature Struct. Biol. 1, 584-590.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 8
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L. & Ernst, R. R. (1983). Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 9
    • 0027492170 scopus 로고
    • A partially folded state of hen egg white lysozyme in trifluoroethanol: Structural characterization and implications for protein folding
    • Buck, M., Radford, S. E. & Dobson, C. M. (1993). A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding. Biochemistry, 32, 669-678.
    • (1993) Biochemistry , vol.32 , pp. 669-678
    • Buck, M.1    Radford, S.E.2    Dobson, C.M.3
  • 10
    • 0028349704 scopus 로고
    • Amide hydrogen exchange in a highly denatured state of hen egg-white lysozyme in urea
    • Buck, M., Radford, S. E. & Dobson, C. M. (1994). Amide hydrogen exchange in a highly denatured state of hen egg-white lysozyme 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
  • 12
    • 33845378943 scopus 로고
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am. Chem. Soc. 107, 2821-2823.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2821-2823
    • Davis, D.G.1    Bax, A.2
  • 13
    • 0022555890 scopus 로고
    • Internal motion of proteins: Nuclear magnetic resonance measurements and dynamics simulations
    • Dobson, C. M. & Karplus, M. (1986). Internal motion of proteins: nuclear magnetic resonance measurements and dynamics simulations. Methods Enzymol. 131, 362-389.
    • (1986) Methods Enzymol. , vol.131 , pp. 362-389
    • Dobson, C.M.1    Karplus, M.2
  • 14
    • 0028053187 scopus 로고
    • Understanding how proteins fold - The lysozyme story so far
    • Dobson, C. M., Evans, P. A. & Radford, S. E. (1994). Understanding how proteins fold - the lysozyme story so far. Trends Biochem. Sci. 19, 31-37.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 31-37
    • Dobson, C.M.1    Evans, P.A.2    Radford, S.E.3
  • 15
    • 0025904730 scopus 로고
    • Defining solution conformations of small linear peptides
    • Dyson, H. J. & Wright, P. E. (1991). Defining solution conformations of small linear peptides. Annu. Rev. Biophys. Biophys. Chem. 20, 519-538.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 519-538
    • Dyson, H.J.1    Wright, P.E.2
  • 16
  • 17
    • 0024278572 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. II The nascent helix
    • Dyson, H. J., Rance, M., Houghten, R. A., Wright, P. E. & Lerner, R. A. (1988). Folding of immunogenic peptide fragments of proteins in water solution. II The nascent helix. J. Mol. Biol. 201, 201-217.
    • (1988) J. Mol. Biol. , vol.201 , pp. 201-217
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Wright, P.E.4    Lerner, R.A.5
  • 18
    • 0026768829 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin
    • Dyson, H. J., Merutka, G., Waltho, J. P., Lerner, R. A. & Wright, P. E. (1992a). Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J. Mol. Biol. 226, 795-817.
    • (1992) J. Mol. Biol. , vol.226 , pp. 795-817
    • Dyson, H.J.1    Merutka, G.2    Waltho, J.P.3    Lerner, R.A.4    Wright, P.E.5
  • 19
    • 0026743136 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. II. Plastocyanin
    • Dyson, H. J., Sayre, J. R., Merutka, G., Shin, H-C., Lerner, R. A. & Wright, P. E. (1992b). Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. II. Plastocyanin. J. Mol. Biol. 226, 819-835.
    • (1992) J. Mol. Biol. , vol.226 , pp. 819-835
    • Dyson, H.J.1    Sayre, J.R.2    Merutka, G.3    Shin, H.-C.4    Lerner, R.A.5    Wright, P.E.6
  • 20
    • 0000749460 scopus 로고    scopus 로고
    • Towards a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements
    • Fiebig, K. M., Schwalbe, H., Buck, M., Smith, L. J. & Dobson, C. M. (1996). Towards a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements. J. Phys. Chem. 100, 2661-2666.
    • (1996) J. Phys. Chem. , vol.100 , pp. 2661-2666
    • Fiebig, K.M.1    Schwalbe, H.2    Buck, M.3    Smith, L.J.4    Dobson, C.M.5
  • 21
    • 0027404071 scopus 로고
    • Stabilization of α-helical structures in short peptides via end capping
    • Forood, B., Feliciano, E. J. & Nambiar, K. P. (1993). Stabilization of α-helical structures in short peptides via end capping. Proc. Natl Acad. Sci. USA, 90, 838-842.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 838-842
    • Forood, B.1    Feliciano, E.J.2    Nambiar, K.P.3
  • 23
  • 24
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimesional NMR spectroscopy
    • Jeener, J., Meier, B. H., Bachmann, P. & Ernst, R. R. (1979). Investigation of exchange processes by two-dimesional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 25
    • 0028301327 scopus 로고
    • NMR solution structure of the isolated N-terminal fragment of protein-GB-1 domain - Evidence of trifluoroethanol induced native-like β-hairpin formation
    • Jimenez, M. A., Pineda, A., Rico, M., Santoro, J. & Nieto, J. L. (1994). NMR solution structure of the isolated N-terminal fragment of protein-GB-1 domain - evidence of trifluoroethanol induced native-like β-hairpin formation. Biochemistry, 33, 6004-6014.
    • (1994) Biochemistry , vol.33 , pp. 6004-6014
    • Jimenez, M.A.1    Pineda, A.2    Rico, M.3    Santoro, J.4    Nieto, J.L.5
  • 26
    • 0027136215 scopus 로고
    • Conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor (BPTI) and their roles in folding
    • Kemmink, J. & Creighton, T. E. (1993). Conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor (BPTI) and their roles in folding. J. Mol. Biol. 234, 487-496.
    • (1993) J. Mol. Biol. , vol.234 , pp. 487-496
    • Kemmink, J.1    Creighton, T.E.2
  • 27
    • 0028838504 scopus 로고
    • Effects of trifluoroethanol on the conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor
    • Kemmink, J. & Creighton, T. E. (1995). Effects of trifluoroethanol on the conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor. Biochemistry, 34, 12630-12635.
    • (1995) Biochemistry , vol.34 , pp. 12630-12635
    • Kemmink, J.1    Creighton, T.E.2
  • 28
    • 49049150378 scopus 로고
    • Two-dimensional chemical exchange and cross-spectroscopy of coupled nuclear spins
    • Macura, C., Huang, Y., Suter, D. & McIntyre, G. J. (1981). Two-dimensional chemical exchange and cross-spectroscopy of coupled nuclear spins. J. Magn. Reson. 43, 259-281.
    • (1981) J. Magn. Reson. , vol.43 , pp. 259-281
    • Macura, C.1    Huang, Y.2    Suter, D.3    McIntyre, G.J.4
  • 29
    • 0029207339 scopus 로고
    • 1H chemical shifts obtained as a function of temperature and trifluroethanol concentration for the peptide series GGXGG
    • 1H chemical shifts obtained as a function of temperature and trifluroethanol concentration for the peptide series GGXGG. J. Biomol. NMR, 5, 14-24.
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 30
    • 0027626054 scopus 로고
    • Improved molecular dynamics simulations for the determination of peptide structures
    • Mierke, D. F. & Kessler, H. (1993). Improved molecular dynamics simulations for the determination of peptide structures. Biopolymers, 33, 1003-1017.
    • (1993) Biopolymers , vol.33 , pp. 1003-1017
    • Mierke, D.F.1    Kessler, H.2
  • 31
    • 0028026122 scopus 로고
    • Peptide flexibility and calculations of an ensemble of molecules
    • Mierke, D. F., Kurz, M. & Kessler, H. (1994). Peptide flexibility and calculations of an ensemble of molecules. J. Am. Chem. Soc. 116, 1042-1049.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 1042-1049
    • Mierke, D.F.1    Kurz, M.2    Kessler, H.3
  • 32
    • 0028568650 scopus 로고
    • Intrinsic secondary structure propensities of the amino acids, using statistical Φ-Ψ matrices: Comparison with experimental scales
    • Munoz, V. & Serrano, L. (1994). Intrinsic secondary structure propensities of the amino acids, using statistical Φ-Ψ matrices: comparison with experimental scales. Proteins: Struct. Funct. Genet. 20, 301-311.
    • (1994) Proteins: Struct. Funct. Genet. , vol.20 , pp. 301-311
    • Munoz, V.1    Serrano, L.2
  • 33
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz, V. & Serrano, L. (1995). Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245, 275-296.
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 34
    • 0028943608 scopus 로고
    • Structural analysis of peptides encompassing all α-helices of three α/β parallel proteins- Che-Y, flavodoxin and P21-ras. Implications for α helix stability and the folding of α/β parallel proteins
    • Munoz, V., Serrano, L., Jimenez, M. A. & Rico, M. (1995). Structural analysis of peptides encompassing all α-helices of three α/β parallel proteins- Che-Y, flavodoxin and P21-ras. Implications for α helix stability and the folding of α/β parallel proteins. J. Mol. Biol. 247, 648-669.
    • (1995) J. Mol. Biol. , vol.247 , pp. 648-669
    • Munoz, V.1    Serrano, L.2    Jimenez, M.A.3    Rico, M.4
  • 35
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace, C. N., Shirley, B. A., McNutt, M. & Gajiwala, K. (1996). Forces contributing to the conformational stability of proteins. FASEB J. 10, 75-83.
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 36
    • 0029653893 scopus 로고
    • Insights into protein-folding using physical techniques - Studies of lysozyme and α-lactalbumin
    • Radford, S. E. & Dobson, C. M. (1995). Insights into protein-folding using physical techniques - studies of lysozyme and α-lactalbumin. Phil. Trans. Roy. Soc. ser. B, 348, 17-25.
    • (1995) Phil. Trans. Roy. Soc. Ser. B , vol.348 , pp. 17-25
    • Radford, S.E.1    Dobson, C.M.2
  • 37
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S. E., Dobson, C. M. & Evans, P. A. (1992a). 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
  • 40
    • 0002445464 scopus 로고
    • Resonance assignment in proteins
    • Roberts, G. K. C., ed., IRL Press at Oxford University Press, Oxford, UK
    • Redfield, C. (1993). Resonance assignment in proteins. In NMR of Macromolecules: A Practical Approach (Roberts, G. K. C., ed.), pp. 71-99, IRL Press at Oxford University Press, Oxford, UK.
    • (1993) NMR of Macromolecules: A Practical Approach , pp. 71-99
    • Redfield, C.1
  • 41
    • 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
  • 42
    • 0026524198 scopus 로고
    • An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate
    • Sancho, J., Neira, J. L. & Fersht, A. R. (1992). An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate. J. Mol. Biol. 224, 748-758.
    • (1992) J. Mol. Biol. , vol.224 , pp. 748-758
    • Sancho, J.1    Neira, J.L.2    Fersht, A.R.3
  • 44
    • 0028790273 scopus 로고
    • Comparison between the Φ distribution of the amino acids in the protein data base and NMR data indicates that amino acids have various Φ propensities in the random coil conformation
    • Serrano, L. (1995). Comparison between the Φ distribution of the amino acids in the protein data base and NMR data indicates that amino acids have various Φ propensities in the random coil conformation. J. Mol. Biol. 254, 322-333.
    • (1995) J. Mol. Biol. , vol.254 , pp. 322-333
    • Serrano, L.1
  • 45
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • Shortle, D. (1996). The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J. 10, 27-34.
    • (1996) FASEB J. , vol.10 , pp. 27-34
    • Shortle, D.1
  • 48
    • 0028774041 scopus 로고
    • Solution structure of a peptide fragment of human α-lactalbumin in trifluoroethanol - A model for local structure in the molten globule
    • Smith, L. J., Alexandrescu, A. T., Pitkeathly, M. & Dobson, C. M. (1994). Solution structure of a peptide fragment of human α-lactalbumin in trifluoroethanol - a model for local structure in the molten globule. Structure, 2, 703-712.
    • (1994) Structure , vol.2 , pp. 703-712
    • Smith, L.J.1    Alexandrescu, A.T.2    Pitkeathly, M.3    Dobson, C.M.4
  • 49
    • 0029978353 scopus 로고    scopus 로고
    • Analysis of main-chain torsion angles in proteins: Prediction of NMR coupling constants for native and random coil conformations
    • Smith, L. J., Bolin, K. A., Schwalbe, H., MacArthur, M. W., Thornton, J. M. & Dobson, C. M. (1996). Analysis of main-chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. J. Mol. Biol. 255, 494-506.
    • (1996) J. Mol. Biol. , vol.255 , pp. 494-506
    • Smith, L.J.1    Bolin, K.A.2    Schwalbe, H.3    MacArthur, M.W.4    Thornton, J.M.5    Dobson, C.M.6
  • 50
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • Sönnichsen, F. D., Van Eyk, J. E., Hodges, R. S. & Sykes, B. D. (1992). Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry, 31, 8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sönnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 51
    • 0027006857 scopus 로고
    • Helix in trifluoroethanol solutions
    • Storrs, R. W., Truckses, D. & Wemmer, D. E. (1992). Helix in trifluoroethanol solutions. Biopolymers, 32, 1695-1702.
    • (1992) Biopolymers , vol.32 , pp. 1695-1702
    • Storrs, R.W.1    Truckses, D.2    Wemmer, D.E.3
  • 52
    • 0029147823 scopus 로고
    • Intrinsic Φ, Ψ propensities of amino acids derived from the coil regions of known structures
    • Swindells, M. B., MacArthur, M. W. & Thornton, J. M. (1995). Intrinsic Φ, Ψ propensities of amino acids derived from the coil regions of known structures. Nature Struct. Biol. 2, 596-603.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 596-603
    • Swindells, M.B.1    MacArthur, M.W.2    Thornton, J.M.3
  • 54
    • 0027165688 scopus 로고
    • Peptide models of protein folding initiation sites. I. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin
    • Waltho, J. P., Feher, V. A., Merutka, G., Dyson, H. J. & Wright, P. E. (1993). Peptide models of protein folding initiation sites. I. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. Biochemistry, 32, 6337-6347.
    • (1993) Biochemistry , vol.32 , pp. 6337-6347
    • Waltho, J.P.1    Feher, V.A.2    Merutka, G.3    Dyson, H.J.4    Wright, P.E.5
  • 55
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D. & Richards, F. M. (1991). Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 58
    • 0021095743 scopus 로고
    • Pseodostructures for the 20 common amino acids for use in studies of protein conformations by measurement of intra molecular proton-proton distance constraints with nuclear magnetic resonance
    • Wüthrich, K., Billeter, M. & Braun, W. (1983). Pseodostructures for the 20 common amino acids for use in studies of protein conformations by measurement of intra molecular proton-proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169, 949-961.
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 59
    • 0027421709 scopus 로고
    • A peptide analog of the calmodulin-binding domain of myosin light chain kinase adopts an α-helical structure in aqueous trifluoroethanol
    • Zhang, M., Yuan, T. & Vogel, H. J. (1993). A peptide analog of the calmodulin-binding domain of myosin light chain kinase adopts an α-helical structure in aqueous trifluoroethanol. Protein Sci. 2, 1931-1937.
    • (1993) Protein Sci. , vol.2 , pp. 1931-1937
    • Zhang, M.1    Yuan, T.2    Vogel, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.