메뉴 건너뛰기




Volumn 29, Issue 10, 2004, Pages 535-541

A common folding mechanism in the cytochrome c family

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C;

EID: 4644231179     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2004.08.004     Document Type: Article
Times cited : (52)

References (51)
  • 1
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • J.D. Bryngelson Funnels, pathways, and the energy landscape of protein folding: a synthesis Proteins Struct. Funct. Genet. 21 1995 167 195
    • (1995) Proteins Struct. Funct. Genet. , vol.21 , pp. 167-195
    • Bryngelson, J.D.1
  • 2
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • A.R. Fersht 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
  • 3
    • 0032734515 scopus 로고    scopus 로고
    • Experiment and theory highlight role of native state topology in SH3 folding
    • D.S. Riddle Experiment and theory highlight role of native state topology in SH3 folding Nat. Struct. Biol. 6 1999 1016 1024
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1016-1024
    • Riddle, D.S.1
  • 4
    • 0032708771 scopus 로고    scopus 로고
    • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    • F. Chiti Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding Nat. Struct. Biol. 6 1999 1005 1009
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1005-1009
    • Chiti, F.1
  • 5
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • J.C. Martinez, and L. Serrano The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved Nat. Struct. Biol. 6 1999 1010 1016
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 6
    • 0031890195 scopus 로고    scopus 로고
    • Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins
    • D. Perl Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins Nat. Struct. Biol. 5 1998 229 235
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 229-235
    • Perl, D.1
  • 7
    • 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
  • 8
    • 0345255608 scopus 로고    scopus 로고
    • Unifying features in protein-folding mechanisms
    • S. Gianni Unifying features in protein-folding mechanisms Proc. Natl. Acad. Sci. U. S. A. 100 2003 13286 13291
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13286-13291
    • Gianni, S.1
  • 9
    • 0033548553 scopus 로고    scopus 로고
    • Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
    • N. Ferguson 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
  • 10
    • 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 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
  • 11
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Y. Bai Protein folding intermediates: native-state hydrogen exchange Science 269 1995 192 197
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1
  • 12
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond time scale
    • M.C. Shastry, and H. Roder Evidence for barrier-limited protein folding kinetics on the microsecond time scale Nat. Struct. Biol. 5 1998 385 392
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.1    Roder, H.2
  • 13
    • 0037675765 scopus 로고    scopus 로고
    • 551 folding
    • 551 folding J. Mol. Biol. 330 2003 1145 1152
    • (2003) J. Mol. Biol. , vol.330 , pp. 1145-1152
    • Gianni, S.1
  • 14
    • 0027131947 scopus 로고
    • Fast events in protein folding initiated by nanosecond laser photolysis
    • C.M. Jones Fast events in protein folding initiated by nanosecond laser photolysis Proc. Natl. Acad. Sci. U. S. A. 90 1993 11860 11864
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 11860-11864
    • Jones, C.M.1
  • 15
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding
    • S.J. Hagen Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding Proc. Natl. Acad. Sci. U. S. A. 93 1996 11615 11617
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 11615-11617
    • Hagen, S.J.1
  • 16
    • 0031952599 scopus 로고    scopus 로고
    • Folding intermediates in cytochrome c
    • S.R. Yeh, and D.L. Rousseau Folding intermediates in cytochrome c Nat. Struct. Biol. 5 1998 222 228
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 222-228
    • Yeh, S.R.1    Rousseau, D.L.2
  • 18
    • 0035793103 scopus 로고    scopus 로고
    • An amino acid code for protein folding
    • J. Rumbley An amino acid code for protein folding Proc. Natl. Acad. Sci. U. S. A. 98 2001 105 112
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 105-112
    • Rumbley, J.1
  • 19
    • 0033603397 scopus 로고    scopus 로고
    • 551: Role of electrostatic interactions on the hydrophobic collapse and transition state properties
    • 551: role of electrostatic interactions on the hydrophobic collapse and transition state properties J. Mol. Biol. 289 1999 1459 1467
    • (1999) J. Mol. Biol. , vol.289 , pp. 1459-1467
    • Travaglini-Allocatelli, C.1
  • 20
    • 0035933343 scopus 로고    scopus 로고
    • 551 from Pseudomonas aeruginosa
    • 551 from Pseudomonas aeruginosa J. Mol. Biol. 309 2001 1177 1187
    • (2001) J. Mol. Biol. , vol.309 , pp. 1177-1187
    • Gianni, S.1
  • 21
    • 0142135083 scopus 로고    scopus 로고
    • 552 from Thermus thermophilus folds through an on-pathway intermediate
    • 552 from Thermus thermophilus folds through an on-pathway intermediate J. Biol. Chem. 278 2003 41136 41140
    • (2003) J. Biol. Chem. , vol.278 , pp. 41136-41140
    • Travaglini-Allocatelli, C.1
  • 22
    • 1842531459 scopus 로고    scopus 로고
    • Cytochrome c folding dynamics
    • J.R. Winkler Cytochrome c folding dynamics Curr. Opin. Chem. Biol. 8 2004 169 174
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 169-174
    • Winkler, J.R.1
  • 23
    • 0034121798 scopus 로고    scopus 로고
    • Stepwise formation of α-helices during cytochrome c folding
    • S. Akiyama Stepwise formation of α-helices during cytochrome c folding Nat. Struct. Biol. 7 2000 514 520
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 514-520
    • Akiyama, S.1
  • 24
    • 0030867722 scopus 로고    scopus 로고
    • 552: A new highly thermostable cytochrome-c structure obtained by MAD phasing
    • 552: a new highly thermostable cytochrome-c structure obtained by MAD phasing J. Mol. Biol. 271 1997 629 644
    • (1997) J. Mol. Biol. , vol.271 , pp. 629-644
    • Than, M.E.1
  • 25
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • G. Wildegger, and T. Kiefhaber 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
  • 26
    • 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 Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation Proc. Natl. Acad. Sci. U. S. A. 101 2004 6450 6455
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6450-6455
    • Jemth, P.1
  • 27
    • 0035170463 scopus 로고    scopus 로고
    • Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate
    • A.P. Capaldi Ultrarapid mixing experiments reveal that Im7 folds via an on-pathway intermediate Nat. Struct. Biol. 8 2001 68 72
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 68-72
    • Capaldi, A.P.1
  • 28
    • 13044284157 scopus 로고    scopus 로고
    • Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c
    • Y. Bai Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c Proc. Natl. Acad. Sci. U. S. A. 96 1999 477 480
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 477-480
    • Bai, Y.1
  • 29
    • 0029967474 scopus 로고    scopus 로고
    • Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding
    • W. Colon Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding Biochemistry 35 1996 5538 5549
    • (1996) Biochemistry , vol.35 , pp. 5538-5549
    • Colon, W.1
  • 30
    • 0031862845 scopus 로고    scopus 로고
    • Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force
    • W.A. McGee, and B.T. Nall Refolding rate of stability-enhanced cytochrome c is independent of thermodynamic driving force Protein Sci. 7 1998 1071 1082
    • (1998) Protein Sci. , vol.7 , pp. 1071-1082
    • McGee, W.A.1    Nall, B.T.2
  • 32
    • 0034713930 scopus 로고    scopus 로고
    • 553, a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics
    • 553, a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics J. Mol. Biol. 301 2000 769 773
    • (2000) J. Mol. Biol. , vol.301 , pp. 769-773
    • Guidry, J.1    Wittung-Stafshede, P.2
  • 33
    • 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 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
  • 34
    • 0032536105 scopus 로고    scopus 로고
    • Native tertiary structure in an A-state
    • J.L. Marmorino Native tertiary structure in an A-state J. Mol. Biol. 275 1998 379 388
    • (1998) J. Mol. Biol. , vol.275 , pp. 379-388
    • Marmorino, J.L.1
  • 35
    • 0032496419 scopus 로고    scopus 로고
    • Protein folding and protein evolution: Common folding nucleus in different subfamilies of c-type cytochromes?
    • O.B. Ptitsyn Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes? J. Mol. Biol. 278 1998 655 666
    • (1998) J. Mol. Biol. , vol.278 , pp. 655-666
    • Ptitsyn, O.B.1
  • 36
    • 5244245983 scopus 로고
    • A correlation of reaction rates
    • G.S. Hammond A correlation of reaction rates J. Am. Chem. Soc. 77 1955 334 339
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 334-339
    • Hammond, G.S.1
  • 37
    • 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
  • 38
    • 0037418635 scopus 로고    scopus 로고
    • Hammond behavior versus ground state effects in protein folding: Evidence for narrow free energy barriers and residual structure in unfolded states
    • I.E. Sanchez, and T. Kiefhaber Hammond behavior versus ground state effects in protein folding: evidence for narrow free energy barriers and residual structure in unfolded states J. Mol. Biol. 327 2003 867 884
    • (2003) J. Mol. Biol. , vol.327 , pp. 867-884
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 39
    • 0034531995 scopus 로고    scopus 로고
    • Selected mutations in a mesophilic cytochrome c confer the stability of a thermophilic counterpart
    • J. Hasegawa Selected mutations in a mesophilic cytochrome c confer the stability of a thermophilic counterpart J. Biol. Chem. 275 2000 37824 37828
    • (2000) J. Biol. Chem. , vol.275 , pp. 37824-37828
    • Hasegawa, J.1
  • 40
    • 0032493312 scopus 로고    scopus 로고
    • 1H-NMR spectroscopy
    • 1H-NMR spectroscopy Biochemistry 37 1998 9641 9649
    • (1998) Biochemistry , vol.37 , pp. 9641-9649
    • Hasegawa, J.1
  • 41
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • V. Muñoz, and L. Serrano Development of the multiple sequence approximation within the AGADIR model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms Biopolymers 41 1997 495 509
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Muñoz, V.1    Serrano, L.2
  • 42
    • 0031866483 scopus 로고    scopus 로고
    • Amide protection in an early folding intermediate of cytochrome c
    • J.M. Sauder, and H. Roder Amide protection in an early folding intermediate of cytochrome c Fold. Des. 3 1998 293 301
    • (1998) Fold. Des. , vol.3 , pp. 293-301
    • Sauder, J.M.1    Roder, H.2
  • 43
    • 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
  • 44
    • 0037456298 scopus 로고    scopus 로고
    • The complete folding pathway of a protein from nanoseconds to microseconds
    • U. Mayor 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
  • 45
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • W.Y. Yang, and M. Gruebele Folding at the speed limit Nature 423 2003 193 197
    • (2003) Nature , vol.423 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2
  • 46
    • 0037073934 scopus 로고    scopus 로고
    • Experimental identification of downhill protein folding
    • M.M. Garcia-Mira Experimental identification of downhill protein folding Science 298 2002 2191 2195
    • (2002) Science , vol.298 , pp. 2191-2195
    • Garcia-Mira, M.M.1
  • 47
    • 0037235662 scopus 로고    scopus 로고
    • Exponential decay kinetics in 'downhill' protein folding
    • S.J. Hagen Exponential decay kinetics in 'downhill' protein folding Proteins 50 2003 1 4
    • (2003) Proteins , vol.50 , pp. 1-4
    • Hagen, S.J.1
  • 48
    • 0034714154 scopus 로고    scopus 로고
    • Two-state expansion and collapse of a polypeptide
    • S.J. Hagen, and W.A. Eaton Two-state expansion and collapse of a polypeptide J. Mol. Biol. 301 2000 1019 1027
    • (2000) J. Mol. Biol. , vol.301 , pp. 1019-1027
    • Hagen, S.J.1    Eaton, W.A.2
  • 49
    • 0037022327 scopus 로고    scopus 로고
    • Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle X-ray scattering
    • S. Akiyama Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle X-ray scattering Proc. Natl. Acad. Sci. U. S. A. 99 2002 1329 1334
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1329-1334
    • Akiyama, S.1
  • 50
    • 0030844583 scopus 로고    scopus 로고
    • Ultrafast signals in protein folding and the polypeptide contracted state
    • T.R. Sosnick Ultrafast signals in protein folding and the polypeptide contracted state Proc. Natl. Acad. Sci. U. S. A. 94 1997 8545 8550
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 8545-8550
    • Sosnick, T.R.1
  • 51
    • 0036440985 scopus 로고    scopus 로고
    • Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding
    • B.A. Krantz Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding J. Mol. Biol. 324 2002 359 371
    • (2002) J. Mol. Biol. , vol.324 , pp. 359-371
    • Krantz, B.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.