메뉴 건너뛰기




Volumn 286, Issue 5, 1999, Pages 1621-1632

The Greek key protein apo-pseudoazurin folds through an obligate on-pathway intermediate

Author keywords

Folding intermediate; Greek key; On pathway; Proline isomerism; Pseudoazurin

Indexed keywords

APOPROTEIN; AZURIN; PROLINE; PSEUDOPEPTIDE; SODIUM SULFATE; UREA;

EID: 0033548458     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2588     Document Type: Article
Times cited : (40)

References (45)
  • 1
    • 0026411154 scopus 로고
    • Copper protein structures
    • Adman E. T. Copper protein structures. Advan. Protein Chem. 42:1991;145-197.
    • (1991) Advan. Protein Chem. , vol.42 , pp. 145-197
    • Adman, E.T.1
  • 2
    • 0030347877 scopus 로고    scopus 로고
    • On-pathway versus off-pathway folding intermediates
    • Baldwin R. L. On-pathway versus off-pathway folding intermediates. Fold. Des. 1:1996;R1-R8.
    • (1996) Fold. Des. , vol.1
    • Baldwin, R.L.1
  • 4
    • 0028402735 scopus 로고
    • The energetic ups and downs of protein-folding
    • Creighton T. E. The energetic ups and downs of protein-folding. Nature Struct. Biol. 1:1994;135-138.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 135-138
    • Creighton, T.E.1
  • 5
    • 0029781355 scopus 로고    scopus 로고
    • The folding mechanism of larger model proteins: Role of native structure
    • Dinner A., Šali A., Karplus M. The folding mechanism of larger model proteins: role of native structure. Proc. Natl Acad. Sci. USA. 93:1996;8356-8361.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8356-8361
    • Dinner, A.1    Šali, A.2    Karplus, M.3
  • 6
    • 0028856785 scopus 로고
    • Optimization of rates of protein-folding - The nucleation-condensation mechanism and its implications
    • Fersht A. R. Optimization of rates of protein-folding - the nucleation-condensation mechanism and its implications. Proc. Natl Acad. Sci. USA. 92:1995;10869-10873.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 7
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht A. R. Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 7:1997;3-9.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 8
    • 0026602877 scopus 로고
    • Comparison of the hemocyanin beta-barrel with other greek key beta-barrels - Possible importance of the beta-zipper in protein-structure and folding
    • Hazes B., Hol W. G. J. Comparison of the hemocyanin beta-barrel with other greek key beta-barrels - possible importance of the beta-zipper in protein-structure and folding. Proteins: Struct. Funct. Genet. 12:1992;278-298.
    • (1992) Proteins: Struct. Funct. Genet. , vol.12 , pp. 278-298
    • Hazes, B.1    Hol, W.G.J.2
  • 9
    • 0030772992 scopus 로고    scopus 로고
    • Evidence for an obligatory intermediate in the folding of interleukin-1 β
    • Heidary D. K., Gross L. A., Roy M., Jennings P. A. Evidence for an obligatory intermediate in the folding of interleukin-1 β Nature Struct. Biol. 4:1997;725-731.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 725-731
    • Heidary, D.K.1    Gross, L.A.2    Roy, M.3    Jennings, P.A.4
  • 11
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson S. E. How do small single-domain proteins fold? Fold. Des. 3:1998;R81-R91.
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 12
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor-2.1. Evidence for a 2-state transition
    • Jackson S. E., Fersht A. R. Folding of chymotrypsin inhibitor-2.1. Evidence for a 2-state transition. Biochemistry. 30:1991;10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 13
    • 0027305989 scopus 로고
    • Folding and stability of a tryptophan-containing mutant of ubiquitin
    • Khorasanizadeh S., Peters I. D., Butt T. R., Roder H. Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry. 32:1993;7054-7063.
    • (1993) Biochemistry , vol.32 , pp. 7054-7063
    • Khorasanizadeh, S.1    Peters, I.D.2    Butt, T.R.3    Roder, H.4
  • 14
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a 3-state model of protein-folding from kinetic-analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh S., Peters I. D., Roder H. Evidence for a 3-state model of protein-folding from kinetic-analysis of ubiquitin variants with altered core residues. Nature Struct. Biol. 3:1996;193-205.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 15
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • Kiefhaber T. Kinetic traps in lysozyme folding. Proc. Natl Acad. Sci. USA. 92:1995;9029-9033.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 16
    • 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
  • 17
    • 0031051445 scopus 로고    scopus 로고
    • The pseudoazurin gene from Thiosphaera pantotropha: Analysis of upstream putative regulatory sequences and overexpression in Escherichia coli
    • Leung Y. C., Chan C., Reader J. S., Willis A. C., van Spanning R. J. M., Ferguson S. J., Radford S. E. The pseudoazurin gene from Thiosphaera pantotropha: analysis of upstream putative regulatory sequences and overexpression in Escherichia coli. Biochem. J. 321:1997;699-705.
    • (1997) Biochem. J. , vol.321 , pp. 699-705
    • Leung, Y.C.1    Chan, C.2    Reader, J.S.3    Willis, A.C.4    Van Spanning, R.J.M.5    Ferguson, S.J.6    Radford, S.E.7
  • 18
    • 0025698613 scopus 로고
    • Transient folding intermediates characterised by protein intermediates
    • Matouschek A., Kellis J. T., Serrano L., Bycroft M., Fersht A. R. Transient folding intermediates characterised by protein intermediates. Nature. 346:1990;440-445.
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis, J.T.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 19
    • 0026550397 scopus 로고
    • The folding of an enzyme. 4. Structure of an intermediate in the refolding of barnase analyzed by a protein engineering procedure
    • Matouschek A., Serrano L., Fersht A. R. The folding of an enzyme. 4. Structure of an intermediate in the refolding of barnase analyzed by a protein engineering procedure. J. Mol. Biol. 224:1992;819-835.
    • (1992) J. Mol. Biol. , vol.224 , pp. 819-835
    • Matouschek, A.1    Serrano, L.2    Fersht, A.R.3
  • 20
    • 0029868655 scopus 로고    scopus 로고
    • Kinetic analysis of the unfolding and refolding of ribonuclease Tl by a stopped-flow double-mixing technique
    • Mayr L. M., Odefey C., Schutkowski M., Schmid F. X. Kinetic analysis of the unfolding and refolding of ribonuclease Tl by a stopped-flow double-mixing technique. Biochemistry. 35:1996;5550-5561.
    • (1996) Biochemistry , vol.35 , pp. 5550-5561
    • Mayr, L.M.1    Odefey, C.2    Schutkowski, M.3    Schmid, F.X.4
  • 21
    • 0027770910 scopus 로고
    • Detection of transient protein folding populations by mass spectrometry
    • Miranker A., Robinson C. V., Radford S. E., Aplin R. T., Dobson C. M. Detection of transient protein folding populations by mass spectrometry. Science. 262:1993;896-899.
    • (1993) Science , vol.262 , pp. 896-899
    • Miranker, A.1    Robinson, C.V.2    Radford, S.E.3    Aplin, R.T.4    Dobson, C.M.5
  • 22
    • 0030334626 scopus 로고    scopus 로고
    • Universality and diversity of the protein folding scenarios: A comprehensive analysis with the aid of a lattice model
    • Mirny L. A., Abkevich V., Shakhnovich E. I. Universality and diversity of the protein folding scenarios: a comprehensive analysis with the aid of a lattice model. Fold. Des. 1:1996;103-116.
    • (1996) Fold. Des. , vol.1 , pp. 103-116
    • Mirny, L.A.1    Abkevich, V.2    Shakhnovich, E.I.3
  • 23
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • Mu ñ V., Thompson P. A., Hofrichter J., Eaton W. A. Folding dynamics and mechanism of β-hairpin formation. Nature. 390:1997;196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Mu Ñ., V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 25
    • 0028870213 scopus 로고
    • Non-prolyl cis-trans peptide-bond isomerization as a rate-determining step in protein unfolding and refolding
    • Odefey C., Mayr L. M., Schmid F. X. Non-prolyl cis-trans peptide-bond isomerization as a rate-determining step in protein unfolding and refolding. J. Mol. Biol. 245:1995;69-78.
    • (1995) J. Mol. Biol. , vol.245 , pp. 69-78
    • Odefey, C.1    Mayr, L.M.2    Schmid, F.X.3
  • 26
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C. N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;3286-3299.
    • (1986) Methods Enzymol. , vol.131 , pp. 3286-3299
    • Pace, C.N.1
  • 27
    • 0030664958 scopus 로고    scopus 로고
    • An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core
    • Park S. H., Oneil K. T., Roder H. An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core. Biochemistry. 36:1997;14277-14283.
    • (1997) Biochemistry , vol.36 , pp. 14277-14283
    • Park, S.H.1    Oneil, K.T.2    Roder, H.3
  • 28
    • 0031010678 scopus 로고    scopus 로고
    • Amide backbone and water-related H/D isotope effects on the dynamics of a protein folding reaction
    • Parker M. J., Clarke A. R. Amide backbone and water-related H/D isotope effects on the dynamics of a protein folding reaction. Biochemistry. 36:1997;5786-5794.
    • (1997) Biochemistry , vol.36 , pp. 5786-5794
    • Parker, M.J.1    Clarke, A.R.2
  • 29
    • 0028791393 scopus 로고
    • An integrated kinetic-analysis of intermediates and transition-states in protein-folding reactions
    • Parker M. J., Spencer J., Clarke A. R. An integrated kinetic-analysis of intermediates and transition-states in protein-folding reactions. J. Mol. Biol. 253:1995;771-786.
    • (1995) J. Mol. Biol. , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clarke, A.R.3
  • 31
    • 0026751786 scopus 로고
    • The flding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford S. E., Dobson C. M., Evans P. A. The flding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:1992;302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 34
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder H., Colón W. Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7:1997;15-28.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colón, W.2
  • 35
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro M., Bolen D. W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.1    Bolen, D.W.2
  • 36
    • 0027730097 scopus 로고
    • Rationally designing the accumulation of a folding intermediate of barnase by protein engineering
    • Sanz J. M., Fersht A. R. Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. Biochemistry. 32:1993;13584-13592.
    • (1993) Biochemistry , vol.32 , pp. 13584-13592
    • Sanz, J.M.1    Fersht, A.R.2
  • 37
    • 0027385015 scopus 로고
    • The refolding of cis -peptidylprolyl and trans -peptidylprolyl isomers of barstar
    • Schreiber G., Fersht A. R. The refolding of cis -peptidylprolyl and trans -peptidylprolyl isomers of barstar. Biochemistry. 32:1993;11195-11203.
    • (1993) Biochemistry , vol.32 , pp. 11195-11203
    • Schreiber, G.1    Fersht, A.R.2
  • 38
    • 0030958760 scopus 로고    scopus 로고
    • Transient aggregates in protein folding are easily mistaken for folding intermediates
    • Silow M., Oliveberg M. Transient aggregates in protein folding are easily mistaken for folding intermediates. Proc. Natl Acad. Sci. USA. 94:1997;6084-6086.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6084-6086
    • Silow, M.1    Oliveberg, M.2
  • 41
    • 0030606223 scopus 로고    scopus 로고
    • Titration properties and thermodynamics of the transition state of folding-comparison of 2-state and multistate folding pathways
    • Tan Y. J., Oliveberg M., Fersht A. R. Titration properties and thermodynamics of the transition state of folding-comparison of 2-state and multistate folding pathways. J. Mol. Biol. 264:1996;377-389.
    • (1996) J. Mol. Biol. , vol.264 , pp. 377-389
    • Tan, Y.J.1    Oliveberg, M.2    Fersht, A.R.3
  • 42
    • 0026666246 scopus 로고
    • Kinetic role of nonnative species in the folding of bovine pancreatic trypsin-inhibitor
    • Weissman J. S., Kim P. S. Kinetic role of nonnative species in the folding of bovine pancreatic trypsin-inhibitor. Proc. Natl Acad. Sci. USA. 89:1992;9900-9904.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 9900-9904
    • Weissman, J.S.1    Kim, P.S.2
  • 43
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Wildegger G., Kiefhaber T. Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate. J. Mol. Biol. 270:1997;294-304.
    • (1997) J. Mol. Biol. , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 44
    • 0028799023 scopus 로고
    • Pseudospecific docking surfaces on electron-transfer proteins as illustrated by pseudoazurin, cytochrome c (550) and cytochrome Cd (1) nitrite reductase
    • Williams P. A., Fülöp V., Leung Y. C., Chan C., Moir J. W. B., Howlett G., Ferguson S. J., Radford S. E., Hajdu J. Pseudospecific docking surfaces on electron-transfer proteins as illustrated by pseudoazurin, cytochrome c (550) and cytochrome Cd (1) nitrite reductase. Nature Struct. Biol. 2:1995;975-982.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 975-982
    • Williams, P.A.1    Fülöp, V.2    Leung, Y.C.3    Chan, C.4    Moir, J.W.B.5    Howlett, G.6    Ferguson, S.J.7    Radford, S.E.8    Hajdu, J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.