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Volumn 353, Issue 2, 2005, Pages 373-384

Engineering stabilising β-sheet interactions into a conformationally flexible region of the folding transition state of ubiquitin

Author keywords

Non native interactions; Protein engineering; Protein folding; Ubiquitin; hairpin stabilisation

Indexed keywords

LEUCINE; MUTANT PROTEIN; PHENYLALANINE; POLYPEPTIDE; SODIUM CHLORIDE; UBIQUITIN;

EID: 25144507750     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.08.044     Document Type: Article
Times cited : (11)

References (60)
  • 1
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and refolding rates of single domain proteins
    • K.W. Plaxco, K.T. Simons, and D. Baker Contact order, transition state placement and refolding rates of single domain proteins J. Mol. Biol. 277 1998 985 994
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 2
  • 3
    • 0033117763 scopus 로고    scopus 로고
    • Matching theory and experiment in protein folding
    • E. Alm, and D. Baker Matching theory and experiment in protein folding Curr. Opin. Struct. Biol. 9 1999 189 196
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 189-196
    • Alm, E.1    Baker, D.2
  • 5
    • 0027382315 scopus 로고
    • Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis
    • S.E. Jackson, N. elMasry, and A.R. Fersht Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis Biochemistry 32 1993 11270 11278
    • (1993) Biochemistry , vol.32 , pp. 11270-11278
    • Jackson, S.E.1    Elmasry, N.2    Fersht, A.R.3
  • 6
    • 0028024928 scopus 로고
    • Specific nucleus as the transition state for protein folding: Evidence from the lattice model
    • V.I. Abkevich, A.M. Gutin, and E.I. Shakhnovich Specific nucleus as the transition state for protein folding: evidence from the lattice model Biochemistry 33 1994 10026 10036
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 7
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-collapse mechanism for protein folding
    • L.S. Itzhaki, D.E. Otzen, and A.R. Fersht The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-collapse 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
  • 8
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • E.I. Shaknovich, V. Abkevich, and O. Ptitsyn Conserved residues and the mechanism of protein folding Nature 379 1996 96 98
    • (1996) Nature , vol.379 , pp. 96-98
    • Shaknovich, E.I.1    Abkevich, V.2    Ptitsyn, O.3
  • 9
    • 0034964196 scopus 로고    scopus 로고
    • Computer-based redesign of a protein folding pathway
    • S. Nauli, B. Kuhlman, and D. Baker Computer-based redesign of a protein folding pathway Nature Struct. Biol. 8 2001 602 605
    • (2001) Nature Struct. Biol. , vol.8 , pp. 602-605
    • Nauli, S.1    Kuhlman, B.2    Baker, D.3
  • 10
    • 0030623698 scopus 로고    scopus 로고
    • Favourable native-like helical local interactions can accelerate protein folding
    • A.R. Viguera, V. Villegas, F.X. Aviles, and L. Serrano Favourable native-like helical local interactions can accelerate protein folding Fold. Des. 2 1997 23 33
    • (1997) Fold. Des. , vol.2 , pp. 23-33
    • Viguera, A.R.1    Villegas, V.2    Aviles, F.X.3    Serrano, L.4
  • 11
  • 12
    • 0031588693 scopus 로고    scopus 로고
    • Folding kinetics of Che Y mutants with enhanced native alpha-helix propensities
    • E. Lopez-Hernandez, P. Cronet, L. Serrano, and V. Munoz Folding kinetics of Che Y mutants with enhanced native alpha-helix propensities J. Mol. Biol. 266 1997 610 620
    • (1997) J. Mol. Biol. , vol.266 , pp. 610-620
    • Lopez-Hernandez, E.1    Cronet, P.2    Serrano, L.3    Munoz, V.4
  • 14
    • 0030627747 scopus 로고    scopus 로고
    • Speeding up protein folding: Mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude
    • M. Munson, K.S. Anderson, and L. Regan Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude Fold. Des. 2 1997 77 87
    • (1997) Fold. Des. , vol.2 , pp. 77-87
    • Munson, M.1    Anderson, K.S.2    Regan, L.3
  • 15
    • 4143061715 scopus 로고    scopus 로고
    • Switching two-state to three-state kinetics in the helical protein Im9 via the optimisation of stabilising non-native interactions by design
    • C.T. Friel, G.S. Beddard, and S.E. Radford Switching two-state to three-state kinetics in the helical protein Im9 via the optimisation of stabilising non-native interactions by design J. Mol. Biol. 342 2004 261 273
    • (2004) J. Mol. Biol. , vol.342 , pp. 261-273
    • Friel, C.T.1    Beddard, G.S.2    Radford, S.E.3
  • 16
    • 0035839115 scopus 로고    scopus 로고
    • Bergerac-SH3: "frustration" induced by stabilising the folding nucleus
    • A.-R. Viguera, and L. Serrano Bergerac-SH3: "frustration" induced by stabilising the folding nucleus J. Mol. Biol. 311 2001 357 371
    • (2001) J. Mol. Biol. , vol.311 , pp. 357-371
    • Viguera, A.-R.1    Serrano, L.2
  • 17
    • 0038286126 scopus 로고    scopus 로고
    • Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterisation of a folding intermediate in equilibrium
    • A.-R. Viguera, and L. Serrano Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterisation of a folding intermediate in equilibrium Proc. Natl Acad. Sci. USA 100 2003 5730 5735
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5730-5735
    • Viguera, A.-R.1    Serrano, L.2
  • 18
    • 3042737819 scopus 로고    scopus 로고
    • Incremental contribution to protein stability from a β-hairpin "finger": Limits on the stability of designed β-hairpin peptides
    • M.S. Searle, G.W. Platt, R. Bofill, S.A. Simpson, and B. Ciani Incremental contribution to protein stability from a β-hairpin "finger": limits on the stability of designed β-hairpin peptides Angew Chem. Int. Ed. 43 2004 1991 1994
    • (2004) Angew Chem. Int. Ed. , vol.43 , pp. 1991-1994
    • Searle, M.S.1    Platt, G.W.2    Bofill, R.3    Simpson, S.A.4    Ciani, B.5
  • 19
    • 18144421515 scopus 로고    scopus 로고
    • Extending the folding nucleus of ubiquitin with an independently folding β-hairpin finger: Hurdles to rapid folding arising from the stabilisation of local interactions
    • R. Bofill, E.R. Simpson, G.W. Platt, M.D. Crespo, and M.S. Searle Extending the folding nucleus of ubiquitin with an independently folding β-hairpin finger: hurdles to rapid folding arising from the stabilisation of local interactions J. Mol. Biol. 349 2005 205 221
    • (2005) J. Mol. Biol. , vol.349 , pp. 205-221
    • Bofill, R.1    Simpson, E.R.2    Platt, G.W.3    Crespo, M.D.4    Searle, M.S.5
  • 20
    • 0037117477 scopus 로고    scopus 로고
    • Unspecific hydrophobic stabilization of folding transition states
    • A.R. Viguera, C. Vega, and L. Serrano Unspecific hydrophobic stabilization of folding transition states Proc. Natl Acad. Sci. USA 99 2002 5349 5354
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5349-5354
    • Viguera, A.R.1    Vega, C.2    Serrano, L.3
  • 21
    • 0035193250 scopus 로고    scopus 로고
    • Diffusion-collision model study of misfolding in a four helix bundle protein
    • C. Beck, X. Siemens, and D.L. Weaver Diffusion-collision model study of misfolding in a four helix bundle protein Biophys. J. 81 2001 3105 3115
    • (2001) Biophys. J. , vol.81 , pp. 3105-3115
    • Beck, C.1    Siemens, X.2    Weaver, D.L.3
  • 22
    • 1042279571 scopus 로고    scopus 로고
    • Comparison of the transition state ensembles for folding of Im7 and Im9 determined using all-atom molecular dynamics simulations with phi value restraints
    • E. Paci, C.T. Friel, K. Lindorff-Larsen, S.E. Radford, M. Karplus, and M. Vendruscolo Comparison of the transition state ensembles for folding of Im7 and Im9 determined using all-atom molecular dynamics simulations with phi value restraints Proteins: Struct. Funct. Genet. 54 2004 513 525
    • (2004) Proteins: Struct. Funct. Genet. , vol.54 , pp. 513-525
    • Paci, E.1    Friel, C.T.2    Lindorff-Larsen, K.3    Radford, S.E.4    Karplus, M.5    Vendruscolo, M.6
  • 23
    • 0035252350 scopus 로고    scopus 로고
    • Three key residues for a critical contact network in a folding transition state
    • M. Vendruscolo, E. Paci, C.M. Dobson, and M. Karplus Three key residues for a critical contact network in a folding transition state Nature 409 2001 641 645
    • (2001) Nature , vol.409 , pp. 641-645
    • Vendruscolo, M.1    Paci, E.2    Dobson, C.M.3    Karplus, M.4
  • 24
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Mis-folding on a path to the native state
    • A.P. Capaldi, C. Kleanthous, and S.E. Radford Im7 folding mechanism: mis-folding on a path to the native state Nature Struct. Biol. 9 2002 209 216
    • (2002) Nature Struct. Biol. , vol.9 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 26
    • 0036500833 scopus 로고    scopus 로고
    • Making a network of hydrophobic clusters
    • R.L. Baldwin Making a network of hydrophobic clusters Science 295 2002 1657 1658
    • (2002) Science , vol.295 , pp. 1657-1658
    • Baldwin, R.L.1
  • 27
    • 0033578940 scopus 로고    scopus 로고
    • A tale of two secondary structure elements: When a β-hairpin becomes an β-helix
    • D. Cregut, C. Civera, M.J. Macias, G. Wallon, and L. Serrano A tale of two secondary structure elements: when a β-hairpin becomes an β-helix J. Mol. Biol. 292 1999 389 401
    • (1999) J. Mol. Biol. , vol.292 , pp. 389-401
    • Cregut, D.1    Civera, C.2    MacIas, M.J.3    Wallon, G.4    Serrano, L.5
  • 28
    • 0027464611 scopus 로고
    • Destabilising effects of replacing a surface lysine of cytochrome c with aromatic amino acids: Implications for the denatured state
    • B.E. Bowler, K. May, T. Zaragoza, P. York, A. Dong, and W.S. Caughey Destabilising effects of replacing a surface lysine of cytochrome c with aromatic amino acids: implications for the denatured state Biochemistry 32 1993 183 190
    • (1993) Biochemistry , vol.32 , pp. 183-190
    • Bowler, B.E.1    May, K.2    Zaragoza, T.3    York, P.4    Dong, A.5    Caughey, W.S.6
  • 29
    • 0032032172 scopus 로고    scopus 로고
    • Surface exposed phenylalanines in the RNP1/RNP2 motif stabilise the cold-shock protein CspB from Bacillus subtilis
    • T. Schindler, D. Perl, P. Graumann, V. Sieber, M.A. Marahiel, and F.X. Schmid Surface exposed phenylalanines in the RNP1/RNP2 motif stabilise the cold-shock protein CspB from Bacillus subtilis Proteins: Struct. Funct. Genet. 30 1998 401 406
    • (1998) Proteins: Struct. Funct. Genet. , vol.30 , pp. 401-406
    • Schindler, T.1    Perl, D.2    Graumann, P.3    Sieber, V.4    Marahiel, M.A.5    Schmid, F.X.6
  • 30
    • 0033006220 scopus 로고    scopus 로고
    • Tolerance of a protein to multiple polar-to-hydrophobic surface substitutions
    • M.H. Cordes, and R.T. Sauer Tolerance of a protein to multiple polar-to-hydrophobic surface substitutions Protein Sci. 8 1999 318 325
    • (1999) Protein Sci. , vol.8 , pp. 318-325
    • Cordes, M.H.1    Sauer, R.T.2
  • 31
    • 0032718386 scopus 로고    scopus 로고
    • Salt-induced detour through compact regions of the protein folding landscape
    • D.E. Otzen, and M. Oliveberg Salt-induced detour through compact regions of the protein folding landscape Proc. Natl Acad. Sci. USA 96 1999 11746 11751
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11746-11751
    • Otzen, D.E.1    Oliveberg, M.2
  • 32
    • 10644261303 scopus 로고    scopus 로고
    • Differences in the folding transition state of ubiquitin indicated by φ and ψ analysis
    • T.R. Sosnick, R.S. Dothager, and B.A. Krantz Differences in the folding transition state of ubiquitin indicated by φ and ψ analysis Proc. Natl Acad. Sci. USA 101 2004 17377 17382
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 17377-17382
    • Sosnick, T.R.1    Dothager, R.S.2    Krantz, B.A.3
  • 33
    • 1442348207 scopus 로고    scopus 로고
    • Discerning the structure and energy of multiple transition states in protein folding using φ-analysis
    • B.A. Krantz, R.S. Dothager, and T.R. Sosnick Discerning the structure and energy of multiple transition states in protein folding using φ-analysis J. Mol. Biol. 337 2004 463 475
    • (2004) J. Mol. Biol. , vol.337 , pp. 463-475
    • Krantz, B.A.1    Dothager, R.S.2    Sosnick, T.R.3
  • 34
    • 33645537630 scopus 로고    scopus 로고
    • Ubiquitin folds through a highly polarized transition state
    • H.M. Went, and S.E. Jackson Ubiquitin folds through a highly polarized transition state Protein 2004 Eng. 18, 239-246
    • (2004) Protein
    • Went, H.M.1    Jackson, S.E.2
  • 35
    • 0032246263 scopus 로고    scopus 로고
    • Minimal model systems for β-sheet secondary structure in proteins
    • S.H. Gellman Minimal model systems for β-sheet secondary structure in proteins Curr. Opin. Chem. Biol. 2 1998 717 725
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 717-725
    • Gellman, S.H.1
  • 36
    • 0034743055 scopus 로고    scopus 로고
    • Peptide models of protein β-sheets: Design, folding and insights into stabilising weak interactions
    • M.S. Searle Peptide models of protein β-sheets: design, folding and insights into stabilising weak interactions J. Chem. Soc. Perkin Trans. 2 2001 1011 1020
    • (2001) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1011-1020
    • Searle, M.S.1
  • 37
    • 1942531291 scopus 로고    scopus 로고
    • Insights into stabilising weak interactions in designed peptide β-hairpins
    • M.S. Searle Insights into stabilising weak interactions in designed peptide β-hairpins Biopolymers 76 2004 185 195
    • (2004) Biopolymers , vol.76 , pp. 185-195
    • Searle, M.S.1
  • 38
    • 0027305989 scopus 로고
    • Folding and stability of a tryptophan mutant of ubiquitin
    • S. Khorasanizadeh, I.D. Peters, and H. Roder Folding and stability of a tryptophan mutant of ubiquitin Biochemistry 32 1993 7054 7063
    • (1993) Biochemistry , vol.32 , pp. 7054-7063
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 39
    • 0032507251 scopus 로고    scopus 로고
    • Origin of β-hairpin stability in solution: Structural and thermodynamic analysis of the folding of a model peptide supports hydrophobic stabilisation in water
    • A.J. Maynard, G.J. Sharman, and M.S. Searle Origin of β-hairpin stability in solution: structural and thermodynamic analysis of the folding of a model peptide supports hydrophobic stabilisation in water J. Am. Chem. Soc. 120 1998 1996 2007
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1996-2007
    • Maynard, A.J.1    Sharman, G.J.2    Searle, M.S.3
  • 40
    • 0033536659 scopus 로고    scopus 로고
    • Dissecting the stability of a β-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the β-turn and β-strand contributions to folding
    • S.R. Griffiths-Jones, A.J. Maynard, and M.S. Searle Dissecting the stability of a β-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the β-turn and β-strand contributions to folding J. Mol. Biol. 292 1999 1051 1069
    • (1999) J. Mol. Biol. , vol.292 , pp. 1051-1069
    • Griffiths-Jones, S.R.1    Maynard, A.J.2    Searle, M.S.3
  • 41
    • 9644264177 scopus 로고    scopus 로고
    • Context-dependent effects of proline residues on the stability and folding of ubiquitin
    • M.D. Crespo, G.W. Platt, R. Bofill, and M.S. Searle Context-dependent effects of proline residues on the stability and folding of ubiquitin Eur. J. Biochem. 271 2004 4474 4484
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4474-4484
    • Crespo, M.D.1    Platt, G.W.2    Bofill, R.3    Searle, M.S.4
  • 42
    • 0034718524 scopus 로고    scopus 로고
    • Distinguishing between two-state and three-state models for ubiquitin folding
    • B.A. Krantz, and T.R. Sosnick Distinguishing between two-state and three-state models for ubiquitin folding Biochemistry 39 2000 11696 11701
    • (2000) Biochemistry , vol.39 , pp. 11696-11701
    • Krantz, B.A.1    Sosnick, T.R.2
  • 43
    • 2942617191 scopus 로고    scopus 로고
    • Is an intermediate state populated on the folding pathway of ubiquitin?
    • H.M. Went, C.G. Benitez-Cardoza, and S.E. Jackson Is an intermediate state populated on the folding pathway of ubiquitin? FEBS Letters 567 2004 333 338
    • (2004) FEBS Letters , vol.567 , pp. 333-338
    • Went, H.M.1    Benitez-Cardoza, C.G.2    Jackson, S.E.3
  • 45
    • 0034628913 scopus 로고    scopus 로고
    • Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding
    • K.B. Wong, J. Clarke, C.J. Bond, J.L. Neira, S.M. Freund, A.R. Fersht, and V. Daggett Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding J. Mol. Biol. 296 2000 1257 1282
    • (2000) J. Mol. Biol. , vol.296 , pp. 1257-1282
    • Wong, K.B.1    Clarke, J.2    Bond, C.J.3    Neira, J.L.4    Freund, S.M.5    Fersht, A.R.6    Daggett, V.7
  • 46
    • 0036172116 scopus 로고    scopus 로고
    • Hydrophobic core packing in the SH3 domain folding transition state
    • J.G.B. Northey, A. Di Nardo, and A.R. Davidson Hydrophobic core packing in the SH3 domain folding transition state Nature Struct. Biol. 9 2002 126 130
    • (2002) Nature Struct. Biol. , vol.9 , pp. 126-130
    • Northey, J.G.B.1    Di Nardo, A.2    Davidson, A.R.3
  • 47
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • I.E. Sanchez, and T. Kiefhaber Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding J. Mol. Biol. 325 2003 367 376
    • (2003) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 48
    • 0027364930 scopus 로고
    • Dissecting the structure of a partially folded protein. CD and NMR studies of peptides from ubiquitin
    • J.P.L. Cox, P.A. Evans, L.C. Packman, D.H. Williams, and D.N. Woolfson Dissecting the structure of a partially folded protein. CD and NMR studies of peptides from ubiquitin J. Mol. Biol. 234 1993 483 492
    • (1993) J. Mol. Biol. , vol.234 , pp. 483-492
    • Cox, J.P.L.1    Evans, P.A.2    Packman, L.C.3    Williams, D.H.4    Woolfson, D.N.5
  • 50
    • 0028865129 scopus 로고
    • A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin
    • M.S. Searle, D.H. Williams, and L.C. Packman A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin Nature Struct. Biol. 2 1995 999 1006
    • (1995) Nature Struct. Biol. , vol.2 , pp. 999-1006
    • Searle, M.S.1    Williams, D.H.2    Packman, L.C.3
  • 51
    • 0034633950 scopus 로고    scopus 로고
    • Co-operative assembly of a native-like ubiquitin structure through peptide fragment complexation: Energetics of peptide association and folding
    • M. Jourdan, and M.S. Searle Co-operative assembly of a native-like ubiquitin structure through peptide fragment complexation: energetics of peptide association and folding Biochemistry 39 2000 12355 12364
    • (2000) Biochemistry , vol.39 , pp. 12355-12364
    • Jourdan, M.1    Searle, M.S.2
  • 52
    • 10644295536 scopus 로고    scopus 로고
    • Φ Value versus ψ analysis
    • A.R. Fersht Φ Value versus ψ analysis Proc. Natl Acad. Sci. USA 101 2004 17327 17328
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 17327-17328
    • Fersht, A.R.1
  • 53
    • 0345708444 scopus 로고    scopus 로고
    • Stability and folding kinetics of a ubiquitin mutant with a strong propensity for non-native β-hairpin conformation in the unfolded state
    • G.W. Platt, S.A. Simpson, R. Layfield, and M.S. Searle Stability and folding kinetics of a ubiquitin mutant with a strong propensity for non-native β-hairpin conformation in the unfolded state Biochemistry 42 2003 13762 13771
    • (2003) Biochemistry , vol.42 , pp. 13762-13771
    • Platt, G.W.1    Simpson, S.A.2    Layfield, R.3    Searle, M.S.4
  • 54
    • 0001250026 scopus 로고
    • 1H 2D NMR spectra by interactive computer graphics
    • 1H 2D NMR spectra by interactive computer graphics J. Magn. Reson. 84 1989 627 633
    • (1989) J. Magn. Reson. , vol.84 , pp. 627-633
    • Kraulis, P.J.1
  • 55
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 57
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • (Creighton, T. E., ed.) 2nd edit., IRL Press, New York.
    • Pace, N. C. & Scholtz, J. M. (1997). Measuring the conformational stability of a protein. In Protein Structure-A Practical Approach (Creighton, T. E., ed.) 2nd edit., pp. 299-321, IRL Press, New York.
    • (1997) Protein Structure-A Practical Approach , pp. 299-321
    • Pace, N.C.1    Scholtz, J.M.2
  • 58
    • 0033548553 scopus 로고    scopus 로고
    • Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
    • N. Ferguson, A.P. Capaldi, R. James, C. Kleanthous, and S.E. Radford Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9 J. Mol. Biol. 286 1999 1597 1608
    • (1999) J. Mol. Biol. , vol.286 , pp. 1597-1608
    • Ferguson, N.1    Capaldi, A.P.2    James, R.3    Kleanthous, C.4    Radford, S.E.5
  • 59
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2: Evidence for a two-state transition
    • S.E. Jackson, and A.R. Fersht Folding of chymotrypsin inhibitor 2: 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
  • 60
    • 0032799756 scopus 로고    scopus 로고
    • Folding of FKBP12: Pathway of folding and characterisation of the transition state
    • E.R.G. Main, K.F. Fulton, and S.E. Jackson Folding of FKBP12: pathway of folding and characterisation of the transition state J. Mol. Biol. 291 1999 429 444
    • (1999) J. Mol. Biol. , vol.291 , pp. 429-444
    • Main, E.R.G.1    Fulton, K.F.2    Jackson, S.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.