메뉴 건너뛰기




Volumn 43, Issue 1, 2009, Pages 123-133

On the role of some conserved and nonconserved amino acid residues in the transitional state and intermediate of apomyoglobin folding

Author keywords

Apomyoglobin; Folding nucleus; Folding rate; Intermediate state; Protein folding; Transition state

Indexed keywords


EID: 61349122791     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S0026893309010178     Document Type: Article
Times cited : (2)

References (51)
  • 1
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • A. Matouschek J.T. Kellis Jr. L. Serrano A.R. Fersht 1989 Mapping the transition state and pathway of protein folding by protein engineering Nature. 340 122 126
    • (1989) Nature. , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Fersht, A.R.4
  • 2
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • A. Matouschek J.T. Kellis Jr. L. Serrano A.R. Fersht 1990 Transient folding intermediates characterized by protein engineering Nature. 346 440 445
    • (1990) Nature. , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Fersht, A.R.4
  • 3
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analyzed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • L.S. Itzhaki D.T. Otzen A.R. Fersht 1995 The structure of the transition state for folding of chymotrypsin inhibitor 2 analyzed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding J. Mol. Biol. 254 260 288
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.T.2    Fersht, A.R.3
  • 4
    • 0032812796 scopus 로고    scopus 로고
    • Mapping the interactions present in the transition state for unfolding/folding of FKBP12
    • K. Fulton E. Main V. Daggett S. Jackson 1999 Mapping the interactions present in the transition state for unfolding/folding of FKBP12 J. Mol. Biol. 291 445 461
    • (1999) J. Mol. Biol. , vol.291 , pp. 445-461
    • Fulton, K.1    Main, E.2    Daggett, V.3    Jackson, S.4
  • 5
    • 0032708771 scopus 로고    scopus 로고
    • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    • F. Chiti N. Taddei P. White M. Bucciantini F. Magherini M. Stefani C. Dobson 1999 Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding Nature Struct. Biol. 6 1005 1009
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1005-1009
    • Chiti, F.1    Taddei, N.2    White, P.3    Bucciantini, M.4    Magherini, F.5    Stefani, M.6    Dobson, C.7
  • 6
    • 0032515105 scopus 로고    scopus 로고
    • Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain
    • V. Villegas J.C. Martinez F.X. Aviles L. Serrano 1998 Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain J. Mol. Biol. 83 1027 1036
    • (1998) J. Mol. Biol. , vol.83 , pp. 1027-1036
    • Villegas, V.1    Martinez, J.C.2    Aviles, F.X.3    Serrano, L.4
  • 7
    • 0031853167 scopus 로고    scopus 로고
    • Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain
    • V.P. Grantcharova D.S. Riddle J.V. Santiago D. Baker 1998 Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain Nature Struct. Biol. 5 714 720
    • (1998) Nature Struct. Biol. , vol.5 , pp. 714-720
    • Grantcharova, V.P.1    Riddle, D.S.2    Santiago, J.V.3    Baker, D.4
  • 8
    • 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. Schiodt K. Kristiansen J. Knudsen F.M. Poulsen 1999 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. 6 594 601
    • (1999) Nature Struct. Biol. , vol.6 , pp. 594-601
    • Kragelund, B.B.1    Osmark, P.2    Neergaard, T.B.3    Schiodt, J.4    Kristiansen, K.5    Knudsen, J.6    Poulsen, F.M.7
  • 9
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • S.E. Jackson 1998 How do small single-domain proteins fold? Fold. Design. 3 R81 R91
    • (1998) Fold. Design. , vol.3
    • Jackson, S.E.1
  • 10
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • J.C. Martinez L. Serrano 1999 The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved Nature Struct. Biol. 6 1010 1016
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 13
    • 0032566696 scopus 로고    scopus 로고
    • Structural characterization of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxinlike topology
    • E. Steensma C.P.M. van Mierlo 1998 Structural characterization of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxinlike topology J. Mol. Biol. 282 653 666
    • (1998) J. Mol. Biol. , vol.282 , pp. 653-666
    • Steensma, E.1    Van Mierlo, C.P.M.2
  • 14
    • 0028176281 scopus 로고
    • Kinetic characterization of the chemotactic protein from Escherichia coli, CheY: Kinetic analysis of the inverse hydrophobic effect
    • V. Munoz E.M. Lopez M. Jager L. Serrano 1994 Kinetic characterization of the chemotactic protein from Escherichia coli, CheY: Kinetic analysis of the inverse hydrophobic effect Biochemistry 33 5858 5866
    • (1994) Biochemistry , vol.33 , pp. 5858-5866
    • Munoz, V.1    Lopez, E.M.2    Jager, M.3    Serrano, L.4
  • 15
    • 0026579572 scopus 로고
    • The folding of an enzyme: 3. Structure of the transition state for unfolding of barnase analyzed by protein engineering procedure
    • L. Serrano A. Matouschek A.R. Fersht 1992 The folding of an enzyme: 3. Structure of the transition state for unfolding of barnase analyzed by protein engineering procedure J. Mol. Biol. 224 805 818
    • (1992) J. Mol. Biol. , vol.224 , pp. 805-818
    • Serrano, L.1    Matouschek, A.2    Fersht, A.R.3
  • 16
    • 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 L. Serrano 1996 Structure of the transition state for folding of the 129-aa protein CheY resembles that of a smaller protein, CI-2 Fold. Design. 1 43 55
    • (1996) Fold. Design. , vol.1 , pp. 43-55
    • Lopez-Hernandez, E.1    Serrano, L.2
  • 17
    • 0033957144 scopus 로고    scopus 로고
    • Folding of β-sandwich proteins: Three-state transition of a fibronectin type III module
    • E. Cota J. Clarke 2000 Folding of β-sandwich proteins: Three-state transition of a fibronectin type III module Protein Sci. 9 112 120
    • (2000) Protein Sci. , vol.9 , pp. 112-120
    • Cota, E.1    Clarke, J.2
  • 19
    • 0028061408 scopus 로고
    • Compactness of protein molten globules: Temperature-induced structural changes of the apomyoglobin folding intermediate
    • K. Gast H. Damaschun M. Muller-Frohne D. Zirwer G. Damaschun 1994 Compactness of protein molten globules: Temperature-induced structural changes of the apomyoglobin folding intermediate Eur. Biophys. J. 23 297 306
    • (1994) Eur. Biophys. J. , vol.23 , pp. 297-306
    • Gast, K.1    Damaschun, H.2    Muller-Frohne, M.3    Zirwer, D.4    Damaschun, G.5
  • 20
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • D. Eliezer P.E. Wright 1996 Is apomyoglobin a molten globule? Structural characterization by NMR J. Mol. Biol. 263 531 538
    • (1996) J. Mol. Biol. , vol.263 , pp. 531-538
    • Eliezer, D.1    Wright, P.E.2
  • 21
    • 0028329347 scopus 로고
    • Thermodynamic puzzle of apomyoglobin unfolding
    • Y.V. Griko P.L. Privalov 1994 Thermodynamic puzzle of apomyoglobin unfolding J. Mol. Biol. 235 1318 1325
    • (1994) J. Mol. Biol. , vol.235 , pp. 1318-1325
    • Griko, Y.V.1    Privalov, P.L.2
  • 22
    • 0030056766 scopus 로고    scopus 로고
    • The native state of apomyoglobin described by proton NMR spectroscopy: The A-B-G-H interface of wild-type sperm whale apomyoglobin
    • M.J. Cocco J.T. Lecomte 1996 The native state of apomyoglobin described by proton NMR spectroscopy: The A-B-G-H interface of wild-type sperm whale apomyoglobin Proteins. 25 267 285
    • (1996) Proteins. , vol.25 , pp. 267-285
    • Cocco, M.J.1    Lecomte, J.T.2
  • 23
    • 0032011922 scopus 로고    scopus 로고
    • Stability and cooperative properties of partially folded proteins
    • W. Pfeil 1998 Stability and cooperative properties of partially folded proteins Biokhimiya. 63 349 359
    • (1998) Biokhimiya. , vol.63 , pp. 349-359
    • Pfeil, W.1
  • 24
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • P.A. Jennings P.E. Wright 1993 Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin Science. 262 292 398
    • (1993) Science. , vol.262 , pp. 292-398
    • Jennings, P.A.1    Wright, P.E.2
  • 25
    • 0024338305 scopus 로고
    • Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates
    • F.M. Hughson R.L. Baldwin 1989 Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates Biochemistry. 28 4415 4422
    • (1989) Biochemistry. , vol.28 , pp. 4415-4422
    • Hughson, F.M.1    Baldwin, R.L.2
  • 26
    • 0025891257 scopus 로고
    • Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis
    • F.M. Hughson D. Barrick R.L. Baldwin 1991 Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis Biochemistry. 30 4113 4118
    • (1991) Biochemistry. , vol.30 , pp. 4113-4118
    • Hughson, F.M.1    Barrick, D.2    Baldwin, R.L.3
  • 27
    • 0242321015 scopus 로고    scopus 로고
    • Role of the B helix in early folding events in apomyoglobin: Evidence from site-directed mutagenesis for native-like long range interactions
    • Ch. Nishimura P.E. Wright H.J. Dyson 2003 Role of the B helix in early folding events in apomyoglobin: Evidence from site-directed mutagenesis for native-like long range interactions J. Mol. Biol. 334 293 307
    • (2003) J. Mol. Biol. , vol.334 , pp. 293-307
    • Nishimura, Ch.1    Wright, P.E.2    Dyson, H.J.3
  • 28
    • 28844466085 scopus 로고    scopus 로고
    • Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin
    • Ch. Nishimura H.J. Dyson P.E. Wright 2006 Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin J. Mol. Biol. 355 139 156
    • (2006) J. Mol. Biol. , vol.355 , pp. 139-156
    • Nishimura, Ch.1    Dyson, H.J.2    Wright, P.E.3
  • 29
    • 0032549072 scopus 로고    scopus 로고
    • Two forms of the pH 4 folding intermediate of apomyoglobin
    • M. Jamin R.L. Baldwin 1998 Two forms of the pH 4 folding intermediate of apomyoglobin J. Mol. Biol. 276 491 504
    • (1998) J. Mol. Biol. , vol.276 , pp. 491-504
    • Jamin, M.1    Baldwin, R.L.2
  • 30
    • 0032901420 scopus 로고    scopus 로고
    • Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate
    • V. Tsui C. Garcia S. Cavagnero G. Siuzdak H.J. Dyson P.E. Wright 1999 Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate Protein Sci. 8 45 49
    • (1999) Protein Sci. , vol.8 , pp. 45-49
    • Tsui, V.1    Garcia, C.2    Cavagnero, S.3    Siuzdak, G.4    Dyson, H.J.5    Wright, P.E.6
  • 31
    • 0036382667 scopus 로고    scopus 로고
    • The apomyoglobin folding pathway revisited: Structural heterogeneity in the kinetic burst phase intermediate
    • C. Nishimura H.J. Dyson P.E. Wright 2002 The apomyoglobin folding pathway revisited: Structural heterogeneity in the kinetic burst phase intermediate J. Mol. Biol. 322 483 489
    • (2002) J. Mol. Biol. , vol.322 , pp. 483-489
    • Nishimura, C.1    Dyson, H.J.2    Wright, P.E.3
  • 32
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • E. Shakhnovich V. Abkevich O. Ptitsyn 1996 Conserved residues and the mechanism of protein folding Nature. 379 96 98
    • (1996) Nature. , vol.379 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 33
    • 0033588067 scopus 로고    scopus 로고
    • Non-functional conserved residues in globins and their possible role as a folding nucleus
    • O.B. Ptitsyn K.-L.H. Ting 1999 Non-functional conserved residues in globins and their possible role as a folding nucleus J. Mol. Biol. 291 671 677
    • (1999) J. Mol. Biol. , vol.291 , pp. 671-677
    • Ptitsyn, O.B.1    Ting, K.-L.H.2
  • 34
    • 0033613131 scopus 로고    scopus 로고
    • A theoretical search for folding/unfolding nuclei in three-dimensional protein structures
    • O.V. Galzitskaya A.V. Finkelstein 1999 A theoretical search for folding/unfolding nuclei in three-dimensional protein structures Proc. Natl. Acad. Sci. USA. 96 11299 11304
    • (1999) Proc. Natl. Acad. Sci. USA. , vol.96 , pp. 11299-11304
    • Galzitskaya, O.V.1    Finkelstein, A.V.2
  • 36
    • 0029400889 scopus 로고
    • Overexpression of myoglobin and assignment of the amid, Cα and Cβ resonances
    • P.A. Jennings M.J. Stone P.E. Wright 1995 Overexpression of myoglobin and assignment of the amid, Cα and Cβ resonances J. Biomol. NMR. 6 271 276
    • (1995) J. Biomol. NMR. , vol.6 , pp. 271-276
    • Jennings, P.A.1    Stone, M.J.2    Wright, P.E.3
  • 37
    • 18844461292 scopus 로고
    • Reversible conformational changes of myoglobin and apomyoglobin
    • S.C. Harrison E.R. Blout 1965 Reversible conformational changes of myoglobin and apomyoglobin J. Biol. Chem. 61 623 627
    • (1965) J. Biol. Chem. , vol.61 , pp. 623-627
    • Harrison, S.C.1    Blout, E.R.2
  • 38
    • 61349131401 scopus 로고    scopus 로고
    • PH-Dependent equilibrium unfolding of apomyoglobin: Substitutions at conservative piositions Trp14 and ÃÂt131 and at nonconservative position V‡l17
    • A.E. Dyuisekina D.A. Dolgikh Sarmatova 2008 pH-Dependent equilibrium unfolding of apomyoglobin: Substitutions at conservative piositions Trp14 and ÃÂt131 and at nonconservative position V‡l17 Biokhimiya. 73 863 873
    • (2008) Biokhimiya. , vol.73 , pp. 863-873
    • Dyuisekina, A.E.1    Dolgikh, D.A.2    Sarmatova3
  • 41
    • 0028791393 scopus 로고
    • An integrated kinetic analysis of intermediates and transition states in protein folding reactions
    • M.J. Parker J. Spencer A.R. Clarke 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
  • 42
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • R.L. Baldwin 1996 On-pathway versus off-pathway folding intermediates Fold. Des. 1 R1 R8
    • (1996) Fold. Des. , vol.1
    • Baldwin, R.L.1
  • 45
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • F.M. Hughson P.E. Wright R.L. Baldwin 1990 Structural characterization of a partly folded apomyoglobin intermediate Science. 249 1544 1548
    • (1990) Science. , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 46
    • 0025891257 scopus 로고
    • Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis
    • F.M. Hughson D. Barrick R.L. Baldwin 1991 Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis Biochemistry. 30 4113 4118
    • (1991) Biochemistry. , vol.30 , pp. 4113-4118
    • Hughson, F.M.1    Barrick, D.2    Baldwin, R.L.3
  • 47
    • 0034650515 scopus 로고    scopus 로고
    • The folding pathway of the cell-cycle regulatory protein p13suc1: Clues for the mechanism of domain swapping
    • J. Schymkowitz F. Rousseau L. Irvine L. Itzhaki 2000 The folding pathway of the cell-cycle regulatory protein p13suc1: Clues for the mechanism of domain swapping Struct. Fold. Des. 8 89 100
    • (2000) Struct. Fold. Des. , vol.8 , pp. 89-100
    • Schymkowitz, J.1    Rousseau, F.2    Irvine, L.3    Itzhaki, L.4
  • 49
    • 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 J. Clarke 2001 Mapping the folding pathway of an immunoglobulin domain: Structural detail from phi value analysis and movement of the transition state Structure (Cambridge). 9 355 366
    • (2001) Structure (Cambridge). , vol.9 , pp. 355-366
    • Fowler, S.B.1    Clarke, J.2
  • 50
    • 4344596240 scopus 로고    scopus 로고
    • Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region
    • A.M. Bertagna D. Barrick 2004 Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region Proc. Natl. Acad. Sci. USA. 101 12514 12519
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 12514-12519
    • Bertagna, A.M.1    Barrick, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.