메뉴 건너뛰기




Volumn 344, Issue 1, 2004, Pages 207-221

The folding of spectrin domains II: Phi-value analysis of R16

Author keywords

chevron plot; curvature; phi value; protein folding; spectrin

Indexed keywords

FODRIN; SPECTRIN;

EID: 7044222120     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.09.023     Document Type: Article
Times cited : (57)

References (68)
  • 1
    • 7044231679 scopus 로고    scopus 로고
    • Taking snapshots of cobalt(III) cytochrome c folding: Real-time NMR studies
    • E.V. Pletneva, D.B. Fulton, J.R. Winkler, and H.B. Gray Taking snapshots of cobalt(III) cytochrome c folding: real-time NMR studies J. Inorg. Biochem. 96 2003 211
    • (2003) J. Inorg. Biochem. , vol.96 , pp. 211
    • Pletneva, E.V.1    Fulton, D.B.2    Winkler, J.R.3    Gray, H.B.4
  • 2
    • 0242578172 scopus 로고    scopus 로고
    • Intimate view of a kinetic protein folding intermediate: Residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity
    • M.M.G. Krishna, Y. Lin, L. Mayne, and S.W. Englander Intimate view of a kinetic protein folding intermediate: residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity J. Mol. Biol. 334 2003 501 513
    • (2003) J. Mol. Biol. , vol.334 , pp. 501-513
    • Krishna, M.M.G.1    Lin, Y.2    Mayne, L.3    Englander, S.W.4
  • 4
    • 0036293508 scopus 로고    scopus 로고
    • The cytochrome c folding landscape revealed by electron- transfer kinetics
    • J.C. Lee, I.J. Chang, H.B. Gray, and J.R. Winkler The cytochrome c folding landscape revealed by electron- transfer kinetics J. Mol. Biol. 320 2002 159 164
    • (2002) J. Mol. Biol. , vol.320 , pp. 159-164
    • Lee, J.C.1    Chang, I.J.2    Gray, H.B.3    Winkler, J.R.4
  • 5
    • 0031095826 scopus 로고    scopus 로고
    • Rate of intrachain diffusion of unfolded cytochrome c
    • S.J. Hagen, J. Hofrichter, and W.A. Eaton Rate of intrachain diffusion of unfolded cytochrome c J. Phys. Chem. B 101 1997 2352 2365
    • (1997) J. Phys. Chem. B , vol.101 , pp. 2352-2365
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 6
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding
    • S.J. Hagen, J. Hofrichter, A. Szabo, and W.A. Eaton Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding Proc. Natl Acad. Sci. USA 93 1996 11615 11617
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11615-11617
    • Hagen, S.J.1    Hofrichter, J.2    Szabo, A.3    Eaton, W.A.4
  • 8
    • 0033535839 scopus 로고    scopus 로고
    • Cytochrome b(562) folding triggered by electron transfer: Approaching the speed limit for formation of a four-helix- bundle protein
    • P. Wittung-Stafshede, J.C. Lee, J.R. Winkler, and H.B. Gray Cytochrome b(562) folding triggered by electron transfer: approaching the speed limit for formation of a four-helix- bundle protein Proc. Natl Acad. Sci. USA 96 1999 6587 6590
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6587-6590
    • Wittung-Stafshede, P.1    Lee, J.C.2    Winkler, J.R.3    Gray, H.B.4
  • 9
    • 0033587495 scopus 로고    scopus 로고
    • Defining folding and unfolding reactions of apocytochrome b(5) using equilibrium and kinetic fluorescence measurements
    • S. Manyusa, and D. Whitford Defining folding and unfolding reactions of apocytochrome b(5) using equilibrium and kinetic fluorescence measurements Biochemistry 38 1999 9533 9540
    • (1999) Biochemistry , vol.38 , pp. 9533-9540
    • Manyusa, S.1    Whitford, D.2
  • 10
    • 0033607191 scopus 로고    scopus 로고
    • Analysis of folding and unfolding reactions of cytochrome b(5)
    • S. Manyusa, G. Mortuza, and D. Whitford Analysis of folding and unfolding reactions of cytochrome b(5) Biochemistry 38 1999 14352 14362
    • (1999) Biochemistry , vol.38 , pp. 14352-14362
    • Manyusa, S.1    Mortuza, G.2    Whitford, D.3
  • 11
    • 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
    • C. Nishimura, P.E. Wright, and H.J. Dyson 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 2003 293 307
    • (2003) J. Mol. Biol. , vol.334 , pp. 293-307
    • Nishimura, C.1    Wright, P.E.2    Dyson, H.J.3
  • 12
    • 0035957221 scopus 로고    scopus 로고
    • NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding
    • J. Yao, J. Chung, D. Eliezer, P.E. Wright, and H.J. Dyson NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding Biochemistry 40 2001 3561 3571
    • (2001) Biochemistry , vol.40 , pp. 3561-3571
    • Yao, J.1    Chung, J.2    Eliezer, D.3    Wright, P.E.4    Dyson, H.J.5
  • 13
    • 0036382667 scopus 로고    scopus 로고
    • The apomyoglobin folding pathway revisited: Structural heterogeneity in the kinetic burst phase intermediate
    • C. Nishimura, H.J. Dyson, and P.E. Wright The apomyoglobin folding pathway revisited: structural heterogeneity in the kinetic burst phase intermediate J. Mol. Biol. 322 2002 483 489
    • (2002) J. Mol. Biol. , vol.322 , pp. 483-489
    • Nishimura, C.1    Dyson, H.J.2    Wright, P.E.3
  • 14
    • 0033871703 scopus 로고    scopus 로고
    • Conservation of folding pathways in evolutionarily distant globin sequences
    • C. Nishimura, S. Prytulla, H.J. Dyson, and P.E. Wright Conservation of folding pathways in evolutionarily distant globin sequences Nature Struct. Biol. 7 2000 679 686
    • (2000) Nature Struct. Biol. , vol.7 , pp. 679-686
    • Nishimura, C.1    Prytulla, S.2    Dyson, H.J.3    Wright, P.E.4
  • 15
    • 0036428782 scopus 로고    scopus 로고
    • Simulation of folding of a small alpha-helical protein in atomistic detail using worldwide-distributed computing
    • B. Zagrovic, C.D. Snow, M.R. Shirts, and V.S. Pande Simulation of folding of a small alpha-helical protein in atomistic detail using worldwide- distributed computing J. Mol. Biol. 323 2002 927 937
    • (2002) J. Mol. Biol. , vol.323 , pp. 927-937
    • Zagrovic, B.1    Snow, C.D.2    Shirts, M.R.3    Pande, V.S.4
  • 16
    • 0037235952 scopus 로고    scopus 로고
    • Atomistic protein folding simulations on the submillisecond time scale using worldwide distributed computing
    • V.S. Pande, I. Baker, J. Chapman, S.P. Elmer, S. Khaliq, and S.M. Larson Atomistic protein folding simulations on the submillisecond time scale using worldwide distributed computing Biopolymers 68 2003 91 109
    • (2003) Biopolymers , vol.68 , pp. 91-109
    • Pande, V.S.1    Baker, I.2    Chapman, J.3    Elmer, S.P.4    Khaliq, S.5    Larson, S.M.6
  • 17
    • 0036394906 scopus 로고    scopus 로고
    • Native-like mean structure in the unfolded ensemble of small proteins
    • B. Zagrovic, C.D. Snow, S. Khaliq, M.R. Shirts, and V.S. Pande Native-like mean structure in the unfolded ensemble of small proteins J. Mol. Biol. 323 2002 153 164
    • (2002) J. Mol. Biol. , vol.323 , pp. 153-164
    • Zagrovic, B.1    Snow, C.D.2    Khaliq, S.3    Shirts, M.R.4    Pande, V.S.5
  • 18
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
    • Y. Duan, and P.A. Kollman Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution Science 282 1998 740 744
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.A.2
  • 20
    • 0034610360 scopus 로고    scopus 로고
    • Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation
    • U. Mayor, C.M. Johnson, V. Daggett, and A.R. Fersht Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation Proc. Natl Acad. Sci. USA 97 2000 13518 13522
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13518-13522
    • Mayor, U.1    Johnson, C.M.2    Daggett, V.3    Fersht, A.R.4
  • 21
    • 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
  • 22
    • 0030967896 scopus 로고    scopus 로고
    • Exploring the free energy surface of a three-helix bundle protein
    • Z. Guo, C.L. Brooks III, and E.M. Boczko Exploring the free energy surface of a three-helix bundle protein Proc. Natl Acad. Sci. USA 94 1997 10161 10166
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10161-10166
    • Guo, Z.1    Brooks III, C.L.2    Boczko, E.M.3
  • 23
    • 0028326042 scopus 로고
    • Monte carlo simulations of protein folding. II. Application to protein A, ROP and crambin
    • A. Kolinski, and J. Skolnick Monte carlo simulations of protein folding. II. Application to protein A, ROP and crambin Proteins: Struct. Funct. Genet. 18 1994 353 366
    • (1994) Proteins: Struct. Funct. Genet. , vol.18 , pp. 353-366
    • Kolinski, A.1    Skolnick, J.2
  • 24
    • 0034602807 scopus 로고    scopus 로고
    • Staphylococcal protein A: Unfolding pathways, unfolded states, and differences between the B and e domains
    • D.O.V. Alonso, and V. Daggett Staphylococcal protein A: unfolding pathways, unfolded states, and differences between the B and E domains Proc. Natl Acad. Sci. USA 97 2000 133 138
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 133-138
    • Alonso, D.O.V.1    Daggett, V.2
  • 25
    • 0035005366 scopus 로고    scopus 로고
    • Preorganised secondary structure as an important determinant of fast protein folding
    • J.K. Myers, and T.G. Oas Preorganised secondary structure as an important determinant of fast protein folding Nature Struct. Biol. 8 2001 552 558
    • (2001) Nature Struct. Biol. , vol.8 , pp. 552-558
    • Myers, J.K.1    Oas, T.G.2
  • 26
    • 0030755502 scopus 로고    scopus 로고
    • Absence of a stable intermediate on the folding pathway of protein a
    • Y. Bai, A. Karimi, H.J. Dyson, and P.E. Wright Absence of a stable intermediate on the folding pathway of protein A Protein Sci. 6 1997 1449 1457
    • (1997) Protein Sci. , vol.6 , pp. 1449-1457
    • Bai, Y.1    Karimi, A.2    Dyson, H.J.3    Wright, P.E.4
  • 27
    • 0036307683 scopus 로고    scopus 로고
    • Application of the diffusion-collision model to the folding of three-helix bundle proteins
    • S.A. Islam, M. Karplus, and D.L. Weaver Application of the diffusion-collision model to the folding of three-helix bundle proteins J. Mol. Biol. 318 2002 199 215
    • (2002) J. Mol. Biol. , vol.318 , pp. 199-215
    • Islam, S.A.1    Karplus, M.2    Weaver, D.L.3
  • 28
    • 0029965111 scopus 로고    scopus 로고
    • Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family
    • B.B. Kragelund, P. Hojrup, M.S. Jensen, C.K. Schjerling, E. Juul, J. Knudsen, and F.M. Poulsen Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family J. Mol. Biol. 256 1996 187 200
    • (1996) J. Mol. Biol. , vol.256 , pp. 187-200
    • Kragelund, B.B.1    Hojrup, P.2    Jensen, M.S.3    Schjerling, C.K.4    Juul, E.5    Knudsen, J.6    Poulsen, F.M.7
  • 29
    • 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, 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    Schiodt, J.4    Kristiansen, K.5    Knudsen, J.6    Poulsen, F.M.7
  • 30
    • 0037162450 scopus 로고    scopus 로고
    • Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing
    • K. Teilum, K. Maki, B.B. Kragelund, F.M. Poulsen, and H. Roder Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing Proc. Natl Acad. Sci. USA 99 2002 9807 9812
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 9807-9812
    • Teilum, K.1    Maki, K.2    Kragelund, B.B.3    Poulsen, F.M.4    Roder, H.5
  • 31
    • 0037423705 scopus 로고    scopus 로고
    • Structural analysis of the rate-limiting transition states in the folding of lm7 and lm9: 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 lm7 and lm9: 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
  • 32
    • 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
  • 33
    • 0035965128 scopus 로고    scopus 로고
    • Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9
    • S.A. Gorski, A.P. Capaldi, C. Kleanthous, and S.E. Radford Acidic conditions stabilise intermediates populated during the folding of Im7 and Im9 J. Mol. Biol. 312 2001 849 863
    • (2001) J. Mol. Biol. , vol.312 , pp. 849-863
    • Gorski, S.A.1    Capaldi, A.P.2    Kleanthous, C.3    Radford, S.E.4
  • 35
    • 0035896036 scopus 로고    scopus 로고
    • Using chimeric immunity proteins to explore the energy landscape for alpha-helical protein folding
    • N. Ferguson, W. Li, A.P. Capaldi, C. Kleanthous, and S.E. Radford Using chimeric immunity proteins to explore the energy landscape for alpha-helical protein folding J. Mol. Biol. 307 2001 393 405
    • (2001) J. Mol. Biol. , vol.307 , pp. 393-405
    • Ferguson, N.1    Li, W.2    Capaldi, A.P.3    Kleanthous, C.4    Radford, S.E.5
  • 36
    • 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
  • 37
    • 0032843763 scopus 로고    scopus 로고
    • Transition state hetereogeneity in GCN4 coiled coil folding studied using multisite mutations and crosslinking
    • L.B. Moran, J.P. Schneider, A. Kentis, G.A. Reddy, and T.R. Sosnick Transition state hetereogeneity in GCN4 coiled coil folding studied using multisite mutations and crosslinking Biochemistry 96 1999 10699 10704
    • (1999) Biochemistry , vol.96 , pp. 10699-10704
    • Moran, L.B.1    Schneider, J.P.2    Kentis, A.3    Reddy, G.A.4    Sosnick, T.R.5
  • 38
    • 0035191642 scopus 로고    scopus 로고
    • Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil
    • B.A. Krantz, and T.R. Sosnick Engineered metal binding sites map the heterogeneous folding landscape of a coiled coil Nature Struct. Biol. 8 2001 1042 1047
    • (2001) Nature Struct. Biol. , vol.8 , pp. 1042-1047
    • Krantz, B.A.1    Sosnick, T.R.2
  • 40
    • 0034598940 scopus 로고    scopus 로고
    • Preformed secondary structure drives the association reaction of the GCN4-p1, a model coiled-coil system
    • J.A. Zitzewitz, B. Ibarra-Molero, D.R. Fishel, K.L. Terry, and C.R. Matthews Preformed secondary structure drives the association reaction of the GCN4-p1, a model coiled-coil system J. Mol. Biol. 296 2000 1105 1116
    • (2000) J. Mol. Biol. , vol.296 , pp. 1105-1116
    • Zitzewitz, J.A.1    Ibarra-Molero, B.2    Fishel, D.R.3    Terry, K.L.4    Matthews, C.R.5
  • 41
    • 0028783624 scopus 로고
    • Probing the folding mechanism of a leucine zipper by stopped-flow circular dichroism
    • J.A. Zitzewitz, O. Bilsen, J. Luo, B.E. Jones, and C.R. Matthews Probing the folding mechanism of a leucine zipper by stopped-flow circular dichroism Biochemistry 34 1995 12812 12819
    • (1995) Biochemistry , vol.34 , pp. 12812-12819
    • Zitzewitz, J.A.1    Bilsen, O.2    Luo, J.3    Jones, B.E.4    Matthews, C.R.5
  • 43
    • 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
  • 44
    • 7044226061 scopus 로고    scopus 로고
    • The folding of spectrin domains I. Wild-type domains have the same stability but very different kinetic properties
    • Scott, K. A., Batey, S., Hooten, K. A., Clarke, J. (2004). The folding of spectrin domains I. Wild-type domains have the same stability but very different kinetic properties. J. Mol. Biol. 344 (this issue).
    • (2004) J. Mol. Biol. , vol.344 , Issue.THIS ISSUE
    • Scott, K.A.1    Batey, S.2    Hooten, K.A.3    Clarke, J.4
  • 46
    • 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
  • 47
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidinium hydrochloride denaturation curves
    • C.N. Pace Determination and analysis of urea and guanidinium hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 48
    • 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
  • 49
    • 0037414650 scopus 로고    scopus 로고
    • Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family
    • M.A. Seeliger, S.E. Breward, and L.S. Itzhaki Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the cks family J. Mol. Biol. 325 2003 189 199
    • (2003) J. Mol. Biol. , vol.325 , pp. 189-199
    • Seeliger, M.A.1    Breward, S.E.2    Itzhaki, L.S.3
  • 50
    • 0036293485 scopus 로고    scopus 로고
    • Conformational plasticity in folding of the split beta-alpha-beta protein S6: Evidence for burst-phase disruption of the native state
    • D.E. Otzen, and M. Oliveberg Conformational plasticity in folding of the split beta-alpha-beta 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
  • 51
    • 0035252685 scopus 로고    scopus 로고
    • Characterisation of the transition states for protein folding: Towards a new level of mechanistic detail in protein engineering analysis
    • M. Oliveberg Characterisation of the transition states for protein folding: towards a new level of mechanistic detail in protein engineering analysis Curr. Opin. Struct. Biol. 11 2001 94 100
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 94-100
    • Oliveberg, M.1
  • 52
    • 0000384736 scopus 로고    scopus 로고
    • Alternative explanations for "multistate" kinetics in protein folding: Transient aggregation and changing transition-state ensembles
    • M. Oliveberg Alternative explanations for "multistate" kinetics in protein folding: transient aggregation and changing transition-state ensembles Accts Chem. Res. 31 1998 765 772
    • (1998) Accts Chem. Res. , vol.31 , pp. 765-772
    • Oliveberg, M.1
  • 53
    • 0036298969 scopus 로고    scopus 로고
    • Folding of the yeast prion protein Ure2: Kinetic evidence for folding and unfolding intermediates
    • D. Galani, A.R. Fersht, and S. Perrett Folding of the yeast prion protein Ure2: kinetic evidence for folding and unfolding intermediates J. Mol. Biol. 315 2002 213 227
    • (2002) J. Mol. Biol. , vol.315 , pp. 213-227
    • Galani, D.1    Fersht, A.R.2    Perrett, S.3
  • 54
    • 0033592876 scopus 로고    scopus 로고
    • From snapshot to movie: Phi analysis of protein folding transition states taken one step further
    • T. Ternstrom, U. Mayor, M. Akke, and M. Oliveberg From snapshot to movie: phi 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
    • Ternstrom, T.1    Mayor, U.2    Akke, M.3    Oliveberg, M.4
  • 55
    • 0033580679 scopus 로고    scopus 로고
    • Structural changes in the transition state of protein folding: Alternative interpretations of curved chevron plots
    • D.E. Otzen, O. Kristensen, M. Proctor, and M. Oliveberg Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots Biochemistry 38 1999 6499 6511
    • (1999) Biochemistry , vol.38 , pp. 6499-6511
    • Otzen, D.E.1    Kristensen, O.2    Proctor, M.3    Oliveberg, M.4
  • 56
    • 0032503027 scopus 로고    scopus 로고
    • The changing nature of the protein folding transition state: Implications for the shape of the free-energy profile for folding
    • M. Oliveberg, Y.J. Tan, M. Silow, and A.R. Fersht The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding J. Mol. Biol. 277 1998 933 943
    • (1998) J. Mol. Biol. , vol.277 , pp. 933-943
    • Oliveberg, M.1    Tan, Y.J.2    Silow, M.3    Fersht, A.R.4
  • 57
    • 0035895436 scopus 로고    scopus 로고
    • Apparent two-state tendamistat folding is a sequential process along a defined route
    • A. Bachmann, and T. Kiefhaber Apparent two-state tendamistat folding is a sequential process along a defined route J. Mol. Biol. 306 2001 375 386
    • (2001) J. Mol. Biol. , vol.306 , pp. 375-386
    • Bachmann, A.1    Kiefhaber, T.2
  • 58
    • 0029863942 scopus 로고    scopus 로고
    • The spectrin repeat folds into a three-helix bundle in solution
    • J. Pascual, M. Pfuhl, G. Rivas, A. Pastore, and M. Saraste The spectrin repeat folds into a three-helix bundle in solution FEBS Letters 383 1996 201 207
    • (1996) FEBS Letters , vol.383 , pp. 201-207
    • Pascual, J.1    Pfuhl, M.2    Rivas, G.3    Pastore, A.4    Saraste, M.5
  • 59
    • 0345304461 scopus 로고    scopus 로고
    • Origin of unusual Φ-values in protein folding: Evidence against specific nucleation sites
    • I.E. Sanchez, and T. Kiefhaber Origin of unusual Φ-values in protein folding: evidence against specific nucleation sites J. Mol. Biol. 334 2003 1077 1085
    • (2003) J. Mol. Biol. , vol.334 , pp. 1077-1085
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 60
    • 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
  • 61
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the agadir model of alpha-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • V. Munoz, and L. Serrano Development of the multiple sequence approximation within the agadir model of alpha-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms Biopolymers 41 1997 495 509
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 62
    • 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
  • 63
    • 0024358426 scopus 로고
    • Mapping the transition-state and pathway of protein folding by protein engineering
    • A. Matouschek, J.T. Kellis, L. Serrano, and A.R. Fersht Mapping the transition-state and pathway of protein folding by protein engineering Nature 340 1989 122 126
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis, J.T.2    Serrano, L.3    Fersht, A.R.4
  • 64
    • 0028037217 scopus 로고
    • Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
    • A.R. Fersht, L.S. Itzhaki, N.F. ElMasry, and J.M. Matthews Single versus parallel pathways of protein folding and fractional formation of structure in the transition state Proc. Natl Acad. Sci. USA 91 1994 10426 10429
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10426-10429
    • Fersht, A.R.1    Itzhaki, L.S.2    Elmasry, N.F.3    Matthews, J.M.4
  • 65
    • 1442348207 scopus 로고    scopus 로고
    • Discerning the structure and energy of multiple transition states in protein folding using Ψ-analysis
    • B.A. Krantz, R.S. Dothager, and T.R. Sosnick Discerning the structure and energy of multiple transition states in protein folding using Ψ-analysis J. Mol. Biol. 377 2004 463 475
    • (2004) J. Mol. Biol. , vol.377 , pp. 463-475
    • Krantz, B.A.1    Dothager, R.S.2    Sosnick, T.R.3
  • 66
    • 85012750408 scopus 로고
    • Kinetic characterisation of complex reaction systems
    • C.H. Bamford C.F.H. Tipper Elsevier Amsterdam
    • Z.G. Szabo Kinetic characterisation of complex reaction systems C.H. Bamford C.F.H. Tipper Comprehensive Chemical Kinetics Vol. 2 1969 Elsevier Amsterdam 1 81
    • (1969) Comprehensive Chemical Kinetics , vol.2 , pp. 1-81
    • Szabo, Z.G.1
  • 67
    • 0026516420 scopus 로고
    • Kinetic coupling between protein folding and prolyl isomerization.1. Theoretical models
    • T. Kiefhaber, H.H. Kohler, and F.X. Schmid Kinetic coupling between protein folding and prolyl isomerization.1. Theoretical models J. Mol. Biol. 224 1992 217 229
    • (1992) J. Mol. Biol. , vol.224 , pp. 217-229
    • Kiefhaber, T.1    Kohler, H.H.2    Schmid, F.X.3
  • 68
    • 0031592935 scopus 로고    scopus 로고
    • Solution structure of the spectrin repeat: A left-handed antiparallel triple-helical coiled-coil
    • J. Pascual, M. Pfuhl, D. Walther, M. Saraste, and M. Nilges Solution structure of the spectrin repeat: a left-handed antiparallel triple-helical coiled-coil J. Mol. Biol. 273 1997 740 751
    • (1997) J. Mol. Biol. , vol.273 , pp. 740-751
    • Pascual, J.1    Pfuhl, M.2    Walther, D.3    Saraste, M.4    Nilges, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.