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Volumn 285, Issue 2, 1999, Pages 741-753

Exploring the conformational properties of the sequence space between two proteins with different folds: An experimental study

Author keywords

Evolution; Modeling; Protein folding; Protein stability; Secondary structure

Indexed keywords

FODRIN; PROTEIN G; SPECTRIN;

EID: 0033555717     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2333     Document Type: Article
Times cited : (41)

References (52)
  • 1
    • 0026782853 scopus 로고
    • Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G
    • Alexander P., Orban J., Bryan P. Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G. Biochemistry. 31:1992a;7243-7248.
    • (1992) Biochemistry , vol.31 , pp. 7243-7248
    • Alexander, P.1    Orban, J.2    Bryan, P.3
  • 2
    • 0026764471 scopus 로고
    • Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures
    • Alexander P., Fhanestock S., Lee T., Orban J., Bryan P. Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures. Biochemistry. 31:1992b;3597-3603.
    • (1992) Biochemistry , vol.31 , pp. 3597-3603
    • Alexander, P.1    Fhanestock, S.2    Lee, T.3    Orban, J.4    Bryan, P.5
  • 3
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A., Davis D. G. MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:1985;355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 4
    • 0031029551 scopus 로고    scopus 로고
    • Protein design: The choice of de novo sequences
    • Beasley J. R., Hecht M. H. Protein design: the choice of de novo sequences. J. Biol. Chem. 272:1997;2031-2034.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2031-2034
    • Beasley, J.R.1    Hecht, M.H.2
  • 5
    • 0029070488 scopus 로고
    • Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements
    • Blanco F. J., Serrano L. Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements. Eur. J. Biochem. 230:1995;634-649.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 634-649
    • Blanco, F.J.1    Serrano, L.2
  • 6
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native stable β-hairpin in aqueous solution
    • Blanco F. J., Rivas G., Serrano L. A short linear peptide that folds into a native stable β-hairpin in aqueous solution. Nature Struct. Biol. 1:1994;584-590.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 7
    • 0031160370 scopus 로고    scopus 로고
    • 15N assignment and solution structure of the SH3 domain of spectrin: Comparison of unrefined and refined structure sets with the crystal structure
    • 15N assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure. J. Biomol. NMR. 9:1997;347-357.
    • (1997) J. Biomol. NMR , vol.9 , pp. 347-357
    • Blanco, F.J.1    Ramírez, A.2    Serrano, L.3
  • 8
    • 0025363984 scopus 로고
    • Deciphering the message in protein sequences: Tolerance to amino acid substitutions
    • Bowie J. U., Reidhaar-Olson J. F., Lim W. A., Sauer R. T. Deciphering the message in protein sequences: tolerance to amino acid substitutions. Science. 247:1990;1306-1310.
    • (1990) Science , vol.247 , pp. 1306-1310
    • Bowie, J.U.1    Reidhaar-Olson, J.F.2    Lim, W.A.3    Sauer, R.T.4
  • 11
    • 84985733652 scopus 로고
    • 1H-NMR parameters of the common amino acid residues measured in aqueous solution of the linear tetrapeptides H-Gly-Gly-X-L-Alα-0H
    • 1H-NMR parameters of the common amino acid residues measured in aqueous solution of the linear tetrapeptides H-Gly-Gly-X-L-Alα-0H. Biopolymers. 18:1979;285-298.
    • (1979) Biopolymers , vol.18 , pp. 285-298
    • Bundi, A.1    Wüthrich, K.2
  • 17
    • 0022545967 scopus 로고
    • Gene for a immunoglobulin-binding protein from a group G Streptococcus
    • Fahnestock S. R., Alexander P., Nagel J., Filpula D. Gene for a immunoglobulin-binding protein from a group G Streptococcus. J. Bacteriol. 167:1986;870-880.
    • (1986) J. Bacteriol. , vol.167 , pp. 870-880
    • Fahnestock, S.R.1    Alexander, P.2    Nagel, J.3    Filpula, D.4
  • 18
    • 0028354429 scopus 로고
    • Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR
    • Gallagher T., Alexander P., Bryan P., Gilliland G. L. Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry. 33:1994;4721-4729.
    • (1994) Biochemistry , vol.33 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 19
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficient from amino acid sequence data
    • Gill S. C., von Hippel P. H. Calculation of protein extinction coefficient from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 20
    • 0031555012 scopus 로고    scopus 로고
    • The foldability landscape of model proteins
    • Govindarajan S., Golstein R. A. The foldability landscape of model proteins. Biopolymers. 42:1997a;427-438.
    • (1997) Biopolymers , vol.42 , pp. 427-438
    • Govindarajan, S.1    Golstein, R.A.2
  • 23
    • 0002281363 scopus 로고
    • The part played by recurrent mutation in evolution
    • Haldane J. B. S. The part played by recurrent mutation in evolution. Am. Nat. 67:1933;5-7.
    • (1933) Am. Nat. , vol.67 , pp. 5-7
    • Haldane, J.B.S.1
  • 24
    • 0022633609 scopus 로고
    • Dideoxy sequencing method using denatured plasmid templates
    • Hattori M., Sasaki Y. Dideoxy sequencing method using denatured plasmid templates. Anal. Biochem. 152:1986;232-238.
    • (1986) Anal. Biochem. , vol.152 , pp. 232-238
    • Hattori, M.1    Sasaki, Y.2
  • 25
    • 0024357799 scopus 로고
    • A simple method for site specific mutagenesis using the polymerase chain reaction
    • Hemsley A. A., Norman M. D., Toney G., Cortopasi, Galas D. A simple method for site specific mutagenesis using the polymerase chain reaction. Nucl. Acids Res. 17:1989;6545-6551.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 6545-6551
    • Hemsley, A.A.1    Norman, M.D.2    Toney, G.3    Cortopasi4    Galas, D.5
  • 26
    • 0023785593 scopus 로고
    • Secondary structure of proteins through circular dichroism spectroscopy
    • Johnson W. C. Secondary structure of proteins through circular dichroism spectroscopy. Annu. Rev. Biophys. Biophys. Chem. 17:1988;145-166.
    • (1988) Annu. Rev. Biophys. Biophys. Chem. , vol.17 , pp. 145-166
    • Johnson, W.C.1
  • 27
    • 0029881326 scopus 로고    scopus 로고
    • Towards meeting the paracelsus challenge: The design, synthesis and characterization of paracelsin-43, an α-helical protein with over 50 % sequence identity to an all-β-protein
    • Jones D. T., Moody C. M., Uppenbrink J., Viles J. H., Doyle P. M., Harris C. J., Pearl L. H., Thornton J. M. Towards meeting the paracelsus challenge: the design, synthesis and characterization of paracelsin-43, an α-helical protein with over 50 % sequence identity to an all-β-protein. Proteins: Struct. Funct. Genet. 24:1996;502-513.
    • (1996) Proteins: Struct. Funct. Genet. , vol.24 , pp. 502-513
    • Jones, D.T.1    Moody, C.M.2    Uppenbrink, J.3    Viles, J.H.4    Doyle, P.M.5    Harris, C.J.6    Pearl, L.H.7    Thornton, J.M.8
  • 28
    • 0028949547 scopus 로고
    • Theoretical studies of protein folding and unfolding
    • Karplus M., Sali A. Theoretical studies of protein folding and unfolding. Curr. Opin. Struct. Biol. 5:1995;58-73.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 58-73
    • Karplus, M.1    Sali, A.2
  • 29
    • 0027411181 scopus 로고
    • Thermodynamic beta-sheet propensities measured using a zinc-finger host peptide
    • Kim C. A., Berg J. M. Thermodynamic beta-sheet propensities measured using a zinc-finger host peptide. Nature. 362:1993;267-270.
    • (1993) Nature , vol.362 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0019327003 scopus 로고
    • A two-dimensional Overhauser effect enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A., Ernst R. R., Wüthrich K. A two-dimensional Overhauser effect enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95:1980;1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 34
    • 0029207339 scopus 로고
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide sries GGXGG
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide sries GGXGG. J. Biomol. NMR. 5:1995;14-24.
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 35
    • 0029155035 scopus 로고
    • Helix design, prediction and stability
    • Mu ñ V., Serrano L. Helix design, prediction and stability. Curr. Opin. Biotech. 6:1995;382-386.
    • (1995) Curr. Opin. Biotech. , vol.6 , pp. 382-386
    • Mu Ñ., V.1    Serrano, L.2
  • 37
    • 0026749753 scopus 로고
    • SH3-an abundant protein domain in search of a function
    • Musacchio A., Gigson T., Lehto V., Saraste M. SH3-an abundant protein domain in search of a function. FEBS Letters. 307:1992a;55-61.
    • (1992) FEBS Letters , vol.307 , pp. 55-61
    • Musacchio, A.1    Gigson, T.2    Lehto, V.3    Saraste, M.4
  • 39
    • 0029983371 scopus 로고    scopus 로고
    • T7 vectors with a modified T7 lac promoter for expression of proteins in Escherichia coli
    • Paränen J., Rikkone M., Hyvónene M., Kääriäinen L. T7 vectors with a modified T7 lac promoter for expression of proteins in Escherichia coli. Anal. Biochem. 236:1996;371-373.
    • (1996) Anal. Biochem. , vol.236 , pp. 371-373
    • Paränen, J.1    Rikkone, M.2    Hyvónene, M.3    Kääriäinen, L.4
  • 40
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini U., Sørensen O. W., Ernst R. R. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104:1982;6800-6801.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sørensen, O.W.2    Ernst, R.R.3
  • 43
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarker G., Sommer S. S. The "megaprimer" method of site-directed mutagenesis. Biotechniques. 8:1990;404-407.
    • (1990) Biotechniques , vol.8 , pp. 404-407
    • Sarker, G.1    Sommer, S.S.2
  • 44
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl M. J. Recognition of errors in three-dimensional structures of proteins. Proteins: Struct. Funct. Genet. 17:1993;355-362.
    • (1993) Proteins: Struct. Funct. Genet. , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 45
    • 0030347890 scopus 로고
    • All-or-none solvent induced transitions between native, molten globule and unfolded states in globular proteins
    • Uversky V. N., Ptitsyn O. B. All-or-none solvent induced transitions between native, molten globule and unfolded states in globular proteins. Folding Design. 1:1995;117-122.
    • (1995) Folding Design , vol.1 , pp. 117-122
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 47
    • 0343059020 scopus 로고
    • Conformational analysis of peptides corresponding to β-hairpins and a β-sheet, that represent the entire sequence of α-spectrin SH3-domain
    • Viguera A. R., Jiminez M. A., Rico M., Serrano L. Conformational analysis of peptides corresponding to β-hairpins and a β-sheet, that represent the entire sequence of α-spectrin SH3-domain. J. Mol. Biol. 255:1995;507-521.
    • (1995) J. Mol. Biol. , vol.255 , pp. 507-521
    • Viguera, A.R.1    Jiminez, M.A.2    Rico, M.3    Serrano, L.4
  • 48
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states may result in the same native structure
    • Viguera A. R., Serrano L., Wilmanns M. Different folding transition states may result in the same native structure. Nature Struct. Biol. 3:1996;874-880.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 49
    • 0025398721 scopus 로고
    • WHATIF: A molecular modelling and drug design program
    • Vriend G. WHATIF: a molecular modelling and drug design program. J. Mol. Graph. 8:1990;52-65.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-65
    • Vriend, G.1
  • 50
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb P. H., Zhen W., Poon A. W., Conway K. A., Lansbury P. T. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry. 35:1996;17709-17715.
    • (1996) Biochemistry , vol.35 , pp. 17709-17715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, P.T.5
  • 52
    • 0032006183 scopus 로고    scopus 로고
    • A hybrid sequence approach to the Pareceluss challenge
    • Yuan S., Clarke N. D. A hybrid sequence approach to the Pareceluss challenge. Proteins: Struct. Funct. Genet. 30:1998;136-143.
    • (1998) Proteins: Struct. Funct. Genet. , vol.30 , pp. 136-143
    • Yuan, S.1    Clarke, N.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.