메뉴 건너뛰기




Volumn 350, Issue 2, 2005, Pages 363-378

The structure of the major transition state for folding of an FF domain from experiment and simulation

Author keywords

FF domain; Molecular dynamics simulation; Phi value analysis; Protein engineering; Protein folding

Indexed keywords

BARNASE;

EID: 20444409471     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.04.067     Document Type: Article
Times cited : (65)

References (74)
  • 1
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • A.R. Fersht, and V. Daggett Protein folding and unfolding at atomic resolution Cell 108 2002 573 582
    • (2002) Cell , vol.108 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 2
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • V. Daggett, and A. Fersht The present view of the mechanism of protein folding Nature Rev. Mol. Cell. Biol. 4 2003 497 502
    • (2003) Nature Rev. Mol. Cell. Biol. , vol.4 , pp. 497-502
    • Daggett, V.1    Fersht, A.2
  • 3
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • S.E. Jackson, and A.R. Fersht Folding of chymotrypsin inhibitor 2. 1. 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
  • 4
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • S.E. Jackson How do small single-domain proteins fold? Fold. Des. 3 1998 81 91
    • (1998) Fold. Des. , vol.3 , pp. 81-91
    • Jackson, S.E.1
  • 5
    • 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.V. 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.V.5    Fersht, A.R.6    Daggett, V.7
  • 6
    • 0036401862 scopus 로고    scopus 로고
    • The expanded denatured state: An ensemble of conformations trapped in a locally encoded topological space
    • D. Shortle The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space Advan. Protein Chem. 62 2002 1 23
    • (2002) Advan. Protein Chem. , vol.62 , pp. 1-23
    • Shortle, D.1
  • 8
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • J.R. Gillespie, and D. Shortle Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures J. Mol. Biol. 268 1997 170 184
    • (1997) J. Mol. Biol. , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 9
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
    • J.R. Gillespie, and D. Shortle Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels J. Mol. Biol. 268 1997 158 169
    • (1997) J. Mol. Biol. , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 10
    • 2542599277 scopus 로고    scopus 로고
    • Φ-Value analysis and the nature of protein-folding transition states
    • A.R. Fersht, and S. Sato Φ-Value analysis and the nature of protein-folding transition states Proc. Natl Acad. Sci. USA 101 2004 7976 7981
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7976-7981
    • Fersht, A.R.1    Sato, S.2
  • 11
    • 0026511656 scopus 로고
    • The folding of an enzyme I. Theory of protein engineering analysis of stability and pathway of protein folding
    • A.R. Fersht, A. Matouschek, and L. Serrano The folding of an enzyme I. Theory of protein engineering analysis of stability and pathway of protein folding J. Mol. Biol. 224 1992 771 782
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 12
    • 2342525803 scopus 로고    scopus 로고
    • Latest folding game result: Protein a barely frustrates computationalists
    • P.G. Wolynes Latest folding game result: protein A barely frustrates computationalists Proc. Natl Acad. Sci. USA 101 2004 6837 6838
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6837-6838
    • Wolynes, P.G.1
  • 13
    • 2342449128 scopus 로고    scopus 로고
    • Testing protein-folding simulations by experiment: B domain of protein a
    • S. Sato, T.L. Religa, V. Daggett, and A.R. Fersht Testing protein-folding simulations by experiment: B domain of protein A Proc. Natl Acad. Sci. USA 101 2004 6952 6956
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6952-6956
    • Sato, S.1    Religa, T.L.2    Daggett, V.3    Fersht, A.R.4
  • 14
    • 0036407694 scopus 로고    scopus 로고
    • The structure of an FF domain from human HYPA/FBP11
    • M. Allen, A. Friedler, O. Schon, and M. Bycroft The structure of an FF domain from human HYPA/FBP11 J. Mol. Biol. 323 2002 411 416
    • (2002) J. Mol. Biol. , vol.323 , pp. 411-416
    • Allen, M.1    Friedler, A.2    Schon, O.3    Bycroft, M.4
  • 15
    • 2342655032 scopus 로고    scopus 로고
    • Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation
    • P. Jemth, S. Gianni, R. Day, B. Li, C.M. Johnson, V. Daggett, and A.R. Fersht Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation Proc. Natl Acad. Sci. USA 101 2004 6450 6455
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6450-6455
    • Jemth, P.1    Gianni, S.2    Day, R.3    Li, B.4    Johnson, C.M.5    Daggett, V.6    Fersht, A.R.7
  • 16
    • 0026579572 scopus 로고
    • The folding of an enzyme III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure
    • L. Serrano, A. Matouschek, and A.R. Fersht The folding of an enzyme III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure J. Mol. Biol. 224 1992 805 818
    • (1992) J. Mol. Biol. , vol.224 , pp. 805-818
    • Serrano, L.1    Matouschek, A.2    Fersht, A.R.3
  • 17
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 18
    • 0014364651 scopus 로고
    • Protein denaturation
    • C. Tanford Protein denaturation Advan. Protein Chem. 23 1968 121 282
    • (1968) Advan. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 20
    • 0037423705 scopus 로고    scopus 로고
    • Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: Similarities and differences in the folding of homologous proteins
    • C.T. Friel, A.P. Capaldi, and S.E. Radford Structural analysis of the rate-limiting transition states in the folding of Im7 and Im9: similarities and differences in the folding of homologous proteins J. Mol. Biol. 326 2003 293 305
    • (2003) J. Mol. Biol. , vol.326 , pp. 293-305
    • Friel, C.T.1    Capaldi, A.P.2    Radford, S.E.3
  • 21
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Misfolding on a path to the native state
    • A.P. Capaldi, C. Kleanthous, and S.E. Radford Im7 folding mechanism: misfolding 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
  • 22
    • 0029041315 scopus 로고
    • Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: Observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase
    • J.M. Matthews, and A.R. Fersht Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase Biochemistry 34 1995 6805 6814
    • (1995) Biochemistry , vol.34 , pp. 6805-6814
    • Matthews, J.M.1    Fersht, A.R.2
  • 23
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation 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-condensation 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
  • 24
    • 0024358426 scopus 로고
    • Mapping the transition state of protein folding by protein engineering
    • A. Matouschek, J.T. Kellis Jr, L. Serrano, and A.R. Fersht Mapping the transition state of protein folding by protein engineering Nature 340 1989 122 126
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Fersht, A.R.4
  • 25
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • A.R. Fersht Characterizing transition states in protein folding: an essential step in the puzzle Curr. Opin. Struct. Biol. 5 1995 79 84
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 26
    • 0029981188 scopus 로고    scopus 로고
    • Structure of the transition state for folding of a protein derived from experiment and simulation
    • V. Daggett, A. Li, L.S. Itzhaki, D.E. Otzen, and A.R. Fersht Structure of the transition state for folding of a protein derived from experiment and simulation J. Mol. Biol. 257 1996 430 440
    • (1996) J. Mol. Biol. , vol.257 , pp. 430-440
    • Daggett, V.1    Li, A.2    Itzhaki, L.S.3    Otzen, D.E.4    Fersht, A.R.5
  • 28
    • 0029963345 scopus 로고    scopus 로고
    • Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations
    • A. Li, and V. Daggett Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations J. Mol. Biol. 257 1996 412 429
    • (1996) J. Mol. Biol. , vol.257 , pp. 412-429
    • Li, A.1    Daggett, V.2
  • 29
    • 14844351260 scopus 로고    scopus 로고
    • Simulation and experiment at high temperatures: Ultrafast folding of a thermophilic protein by nucleation-condensation
    • N. Ferguson, R. Day, C.M. Johnson, M.D. Allen, V. Daggett, and A.R. Fersht Simulation and experiment at high temperatures: ultrafast folding of a thermophilic protein by nucleation-condensation J. Mol. Biol. 347 2005 855 870
    • (2005) J. Mol. Biol. , vol.347 , pp. 855-870
    • Ferguson, N.1    Day, R.2    Johnson, C.M.3    Allen, M.D.4    Daggett, V.5    Fersht, A.R.6
  • 30
    • 0032146792 scopus 로고    scopus 로고
    • Structure-function aspects of prion proteins
    • V. Daggett Structure-function aspects of prion proteins Curr. Opin. Biotechnol. 9 1998 359 365
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 359-365
    • Daggett, V.1
  • 31
    • 0028143603 scopus 로고
    • Characterization of the transition state of protein unfolding by use of molecular dynamics: Chymotrypsin inhibitor 2
    • A. Li, and V. Daggett Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2 Proc. Natl Acad. Sci. USA 91 1994 10430 10434
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10430-10434
    • Li, A.1    Daggett, V.2
  • 32
    • 0032579189 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the unfolding of barnase: Characterization of the major intermediate
    • A. Li, and V. Daggett Molecular dynamics simulation of the unfolding of barnase: characterization of the major intermediate J. Mol. Biol. 275 1998 677 694
    • (1998) J. Mol. Biol. , vol.275 , pp. 677-694
    • Li, A.1    Daggett, V.2
  • 33
    • 0032812796 scopus 로고    scopus 로고
    • Mapping the interactions present in the transition state for unfolding/folding of FKBP12
    • K.F. Fulton, E.R.G. Main, V. Daggett, and S.E. Jackson Mapping the interactions present in the transition state for unfolding/folding of FKBP12 J. Mol. Biol. 291 1999 445 461
    • (1999) J. Mol. Biol. , vol.291 , pp. 445-461
    • Fulton, K.F.1    Main, E.R.G.2    Daggett, V.3    Jackson, S.E.4
  • 34
    • 0342980331 scopus 로고    scopus 로고
    • Characterization of the unfolding pathway of the cell-cycle protein p13suc1 by molecular dynamics simulations: Implications for domain swapping
    • D.O. Alonso, E. Alm, and V. Daggett Characterization of the unfolding pathway of the cell-cycle protein p13suc1 by molecular dynamics simulations: implications for domain swapping Struct. Fold. Des. 8 2000 101 110
    • (2000) Struct. Fold. Des. , vol.8 , pp. 101-110
    • Alonso, D.O.1    Alm, E.2    Daggett, V.3
  • 36
  • 37
    • 0034984382 scopus 로고    scopus 로고
    • Mapping the folding pathway of an immunoglobulin domain: Structural detail from phi value analysis and movement of the transition state
    • S.B. Fowler, and J. Clarke Mapping the folding pathway of an immunoglobulin domain: structural detail from phi value analysis and movement of the transition state Structure 9 2001 355 366
    • (2001) Structure , vol.9 , pp. 355-366
    • Fowler, S.B.1    Clarke, J.2
  • 38
    • 2442683149 scopus 로고    scopus 로고
    • The folding transition state of the cold shock protein is strongly polarized
    • M.M. Garcia-Mira, D. Boehringer, and F.X. Schmid The folding transition state of the cold shock protein is strongly polarized J. Mol. Biol. 339 2004 555 569
    • (2004) J. Mol. Biol. , vol.339 , pp. 555-569
    • Garcia-Mira, M.M.1    Boehringer, D.2    Schmid, F.X.3
  • 39
    • 0034671177 scopus 로고    scopus 로고
    • The SH3-fold family: Experimental evidence and prediction of variations in the folding pathways
    • R. Guerois, and L. Serrano The SH3-fold family: experimental evidence and prediction of variations in the folding pathways J. Mol. Biol. 304 2000 967 982
    • (2000) J. Mol. Biol. , vol.304 , pp. 967-982
    • Guerois, R.1    Serrano, L.2
  • 40
    • 0034677663 scopus 로고    scopus 로고
    • The folding of an immunoglobulin-like Greek-key protein is defined by a common-core nucleus and regions constrained by topology
    • S.J. Hamill, A. Steward, and J. Clarke The folding of an immunoglobulin-like Greek-key protein is defined by a common-core nucleus and regions constrained by topology J. Mol. Biol. 297 2000 165 178
    • (2000) J. Mol. Biol. , vol.297 , pp. 165-178
    • Hamill, S.J.1    Steward, A.2    Clarke, J.3
  • 41
    • 2442659128 scopus 로고    scopus 로고
    • Scattered hammond plots reveal second level of site-specific information in protein folding: Φ′ (β‡)
    • L. Hedberg, and M. Oliveberg Scattered hammond plots reveal second level of site-specific information in protein folding: Φ′ (β‡) Proc. Natl Acad. Sci. USA 101 2004 7606 7611
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7606-7611
    • Hedberg, L.1    Oliveberg, M.2
  • 43
    • 0034685619 scopus 로고    scopus 로고
    • A breakdown of symmetry in the folding transition state of protein L
    • D.E. Kim, C. Fisher, and D. Baker A breakdown of symmetry in the folding transition state of protein L J. Mol. Biol. 298 2000 971 984
    • (2000) J. Mol. Biol. , vol.298 , pp. 971-984
    • Kim, D.E.1    Fisher, C.2    Baker, D.3
  • 44
    • 0033015989 scopus 로고    scopus 로고
    • The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP
    • B.B. Kragelund, P. Osmark, T.B. Neergaard, J. Schiødt, K. Kristiansen, J. Knudsen, and F.M. Poulsen The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP Nature Struct. Biol. 6 1999 594 601
    • (1999) Nature Struct. Biol. , vol.6 , pp. 594-601
    • Kragelund, B.B.1    Osmark, P.2    Neergaard, T.B.3    Schiødt, J.4    Kristiansen, K.5    Knudsen, J.6    Poulsen, F.M.7
  • 45
    • 0036829967 scopus 로고    scopus 로고
    • Complete change of the protein folding transition state upon circular permutation
    • M. Lindberg, J. Tångrot, and M. Oliveberg Complete change of the protein folding transition state upon circular permutation Nature Struct. Biol. 9 2002 818 822
    • (2002) Nature Struct. Biol. , vol.9 , pp. 818-822
    • Lindberg, M.1    Tångrot, J.2    Oliveberg, M.3
  • 46
    • 0030334834 scopus 로고    scopus 로고
    • Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2
    • E. Lopez-Hernandez, and L. Serrano Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2 Fold. Des. 1 1996 43 55
    • (1996) Fold. Des. , vol.1 , pp. 43-55
    • Lopez-Hernandez, E.1    Serrano, L.2
  • 47
    • 0033604845 scopus 로고    scopus 로고
    • Effects of core mutations on the folding of a β-sheet protein: Implications for backbone organization in the I-state
    • M. Lorch, J.M. Mason, A.R. Clarke, and M.J. Parker Effects of core mutations on the folding of a β-sheet protein: implications for backbone organization in the I-state Biochemistry 38 1999 1377 1385
    • (1999) Biochemistry , vol.38 , pp. 1377-1385
    • Lorch, M.1    Mason, J.M.2    Clarke, A.R.3    Parker, M.J.4
  • 48
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • J.C. Martínez, and L. Serrano The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved Nature Struct. Biol. 6 1999 1010 1016
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1010-1016
    • Martínez, J.C.1    Serrano, L.2
  • 49
    • 0037456298 scopus 로고    scopus 로고
    • The complete folding pathway of a protein from nanoseconds to microseconds
    • U. Mayor, N.R. Guydosh, C.M. Johnson, J.G. Grossmann, S. Sato, and G.S. Jas The complete folding pathway of a protein from nanoseconds to microseconds Nature 421 2003 863 867
    • (2003) Nature , vol.421 , pp. 863-867
    • Mayor, U.1    Guydosh, N.R.2    Johnson, C.M.3    Grossmann, J.G.4    Sato, S.5    Jas, G.S.6
  • 50
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of β-hairpin formation in protein G folding
    • E.L. McCallister, E. Alm, and D. Baker Critical role of β-hairpin formation in protein G folding Nature Struct. Biol. 7 2000 669 673
    • (2000) Nature Struct. Biol. , vol.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 51
    • 0028882589 scopus 로고
    • P22 Arc repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding
    • M.E. Milla, B.M. Brown, C.D. Waldburger, and R.T. Sauer P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding Biochemistry 34 1995 13914 13919
    • (1995) Biochemistry , vol.34 , pp. 13914-13919
    • Milla, M.E.1    Brown, B.M.2    Waldburger, C.D.3    Sauer, R.T.4
  • 52
    • 0036172116 scopus 로고    scopus 로고
    • Hydrophobic core packing in the SH3 domain folding transition state
    • J.G.B. Northey, A.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.A.2    Davidson, A.R.3
  • 54
    • 0036293485 scopus 로고    scopus 로고
    • Conformational plasticity in folding of the split β-α-β protein S6: Evidence for burst-phase disruption of the native state
    • D.E. Otzen, and M. Oliveberg Conformational plasticity in folding of the split β-α-β protein S6: evidence for burst-phase disruption of the native state J. Mol. Biol. 317 2002 613 627
    • (2002) J. Mol. Biol. , vol.317 , pp. 613-627
    • Otzen, D.E.1    Oliveberg, M.2
  • 56
    • 7044222120 scopus 로고    scopus 로고
    • The folding of spectrin domains II: Phi-value analysis of R16
    • K.A. Scott, L.G. Randles, and J. Clarke The folding of spectrin domains II: Phi-value analysis of R16 J. Mol. Biol. 344 2004 207 221
    • (2004) J. Mol. Biol. , vol.344 , pp. 207-221
    • Scott, K.A.1    Randles, L.G.2    Clarke, J.3
  • 58
    • 0033592876 scopus 로고    scopus 로고
    • From snapshot to movie: Φ analysis of protein folding transition states taken one step further
    • T. Ternström, U. Mayor, M. Akke, and M. Oliveberg From snapshot to movie: Φ analysis of protein folding transition states taken one step further Proc. Natl Acad. Sci. USA 96 1999 14854 14859
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14854-14859
    • Ternström, T.1    Mayor, U.2    Akke, M.3    Oliveberg, M.4
  • 59
    • 0032515105 scopus 로고    scopus 로고
    • Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain
    • V. Villegas, J.C. Martínez, F.X. Avilés, and L. Serrano Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain J. Mol. Biol. 283 1998 1027 1036
    • (1998) J. Mol. Biol. , vol.283 , pp. 1027-1036
    • Villegas, V.1    Martínez, J.C.2    Avilés, F.X.3    Serrano, L.4
  • 60
    • 0028327236 scopus 로고
    • Protein folding dynamics: The diffusion-collision model and experimental data
    • M. Karplus, and D.L. Weaver Protein folding dynamics: the diffusion-collision model and experimental data Protein Sci. 3 1994 650 668
    • (1994) Protein Sci. , vol.3 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 61
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • R.L. Baldwin, and G.D. Rose Is protein folding hierarchic? II. Folding intermediates and transition states Trends Biochem. Sci. 24 1999 77 83
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 77-83
    • Baldwin, R.L.1    Rose, G.D.2
  • 62
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding
    • V. Daggett, and A.R. Fersht Is there a unifying mechanism for protein folding Trends Biochem. Sci. 28 2003 18 25
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 63
    • 5144225084 scopus 로고    scopus 로고
    • Relationship of Leffler (Brønsted) alpha values and protein folding Phi values to position of transition-state structures on reaction coordinates
    • A.R. Fersht Relationship of Leffler (Brønsted) alpha values and protein folding Phi values to position of transition-state structures on reaction coordinates Proc. Natl Acad. Sci. USA 101 2004 14338 14342
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 14338-14342
    • Fersht, A.R.1
  • 64
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients 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
  • 66
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 67
    • 0023732144 scopus 로고
    • Determinations of the three-dimensional structures of proteins from inter-proton distance data by dynamic simulated annealing from a random array of atoms. Circumventing problems associated with folding
    • M. Nilges, G.M. Clore, and A.M. Gronenborn Determinations of the three-dimensional structures of proteins from inter-proton distance data by dynamic simulated annealing from a random array of atoms. Circumventing problems associated with folding FEBS Letters 239 1988 129 136
    • (1988) FEBS Letters , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 68
    • 0029633167 scopus 로고
    • Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution
    • M. Levitt, M. Hirshberg, R. Sharon, and V. Daggett Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution Comput. Phys. Commun. 91 1995 215 221
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 215-221
    • Levitt, M.1    Hirshberg, M.2    Sharon, R.3    Daggett, V.4
  • 70
    • 0000125216 scopus 로고    scopus 로고
    • Calibration and testing of a water model for simulation of the molecular dynamics of proteins and nucleic acids in solution
    • M. Levitt, M. Hirshberg, R. Sharon, K.E. Laidig, and V. Daggett Calibration and testing of a water model for simulation of the molecular dynamics of proteins and nucleic acids in solution J. Phys. Chem. B 5051 1997 5061
    • (1997) J. Phys. Chem. B , vol.5051 , pp. 5061
    • Levitt, M.1    Hirshberg, M.2    Sharon, R.3    Laidig, K.E.4    Daggett, V.5
  • 72
    • 84887006810 scopus 로고
    • A non-linear mapping for data structure analysis
    • J. Sammon A non-linear mapping for data structure analysis IEEE Trans. Comput. 18 1969 401 409
    • (1969) IEEE Trans. Comput. , vol.18 , pp. 401-409
    • Sammon, J.1
  • 74


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.