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Volumn 380, Issue 7-8, 1999, Pages 923-929

Elementary steps in protein folding

Author keywords

helix; hairpin; Fast kinetics; Intrachain diffusion; Protein folding; Protein loops

Indexed keywords

PROTEIN;

EID: 0032847748     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.1999.114     Document Type: Review
Times cited : (45)

References (64)
  • 1
    • 36448999595 scopus 로고
    • Free energy landscape for protein folding kinetics: Intermediates, traps, and multiple pathways in theory and lattice model simulations
    • Abkevich, V.I., Gutin, A.M., and Shaknovich, E.I. (1994). Free energy landscape for protein folding kinetics: intermediates, traps, and multiple pathways in theory and lattice model simulations. J. Chem. Phys. 101, 6052-6062.
    • (1994) J. Chem. Phys. , vol.101 , pp. 6052-6062
    • Abkevich, V.I.1    Gutin, A.M.2    Shaknovich, E.I.3
  • 2
    • 0026782853 scopus 로고
    • Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of Streptococcal Protein G
    • Alexander, P., Orban, J., and Bryan, P. (1992). Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of Streptococcal Protein G. Biochemistry 31, 7243-7248.
    • (1992) Biochemistry , vol.31 , pp. 7243-7248
    • Alexander, P.1    Orban, J.2    Bryan, P.3
  • 3
    • 0029858841 scopus 로고    scopus 로고
    • Observation of distinct nanosecond and microsecond folding events
    • Ballew, R.M., Sabelko, J., and Gruebele, M. (1996). Observation of distinct nanosecond and microsecond folding events. Nature Struct. Biol. 3, 923-926.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 923-926
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 4
    • 0001106707 scopus 로고
    • Vertical and "nonvertical" energy transfer processes. A general classical treatment
    • Balzani, V., Bolletta, F., and Scandola, F. (1980). Vertical and "nonvertical" energy transfer processes. A general classical treatment. J. Am. Chem. Soc. 102, 2152-2163.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2152-2163
    • Balzani, V.1    Bolletta, F.2    Scandola, F.3
  • 5
    • 0039237901 scopus 로고
    • Dielektrische Absorption als Folge chemischer Relaxation
    • Bergmann, K.M.E., and de Maeyer, L. (1963). Dielektrische Absorption als Folge chemischer Relaxation. Ber. Bunsenges. physikal. Chem. 67, 819-832.
    • (1963) Ber. Bunsenges. Physikal. Chem. , vol.67 , pp. 819-832
    • Bergmann, K.M.E.1    De Maeyer, L.2
  • 8
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson, J.D., and Wolynes, P.G. (1987). Spin glasses and the statistical mechanics of protein folding. Proc. Natl. Acad. Soc. USA 84, 7524-7528.
    • (1987) Proc. Natl. Acad. Soc. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 9
    • 0024733407 scopus 로고
    • Intermediates and barrier crossing in a random model (with applications to protein folding)
    • Bryngelson, J.D., and Wolynes, P.G. (1989). Intermediates and barrier crossing in a random model (with applications to protein folding). J. Phys. Chem. 93, 6902-6915.
    • (1989) J. Phys. Chem. , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 10
    • 0028941444 scopus 로고
    • Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic inhibitor
    • Camacho, C.J., and Thirumalai, D. (1995). Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic inhibitor. Proc. Natl. Acad. Sci. USA 92, 1277-1281.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1277-1281
    • Camacho, C.J.1    Thirumalai, D.2
  • 11
    • 0025804130 scopus 로고
    • Large differences in the helix propensities of alanine and glycine
    • Chakrabartty, A., Schellman, J.A., and Baldwin, R.L. (1991). Large differences in the helix propensities of alanine and glycine. Nature 351, 586-588.
    • (1991) Nature , vol.351 , pp. 586-588
    • Chakrabartty, A.1    Schellman, J.A.2    Baldwin, R.L.3
  • 13
    • 36449000646 scopus 로고
    • Transition states and folding dynamics of proteins and heteropolymers
    • Chan, H.S., and Dill, K.A. (1994). Transition states and folding dynamics of proteins and heteropolymers. J. Chem. Phys. 100, 9238-9257.
    • (1994) J. Chem. Phys. , vol.100 , pp. 9238-9257
    • Chan, H.S.1    Dill, K.A.2
  • 14
    • 0016720521 scopus 로고
    • Helix-coil transition kinetics in aqueous poly(α,L-glutamic acid)
    • Cummings, A.L., and Eyring, E.M. (1975). Helix-coil transition kinetics in aqueous poly(α,L-glutamic acid). Biopolymers 14, 2107-2114.
    • (1975) Biopolymers , vol.14 , pp. 2107-2114
    • Cummings, A.L.1    Eyring, E.M.2
  • 15
    • 0032015332 scopus 로고    scopus 로고
    • Denatures states of yeast phosphoglycerate kinase
    • Moscow
    • Damaschun, G., Damaschun, H., Gast, K., and Zirwer, D. (1998). Denatures states of yeast phosphoglycerate kinase. Biochemistry (Moscow) 63, 259-275.
    • (1998) Biochemistry , vol.63 , pp. 259-275
    • Damaschun, G.1    Damaschun, H.2    Gast, K.3    Zirwer, D.4
  • 16
    • 0032917075 scopus 로고    scopus 로고
    • De novo design of a monomeric three-stranded antiparallel β-sheet
    • de Alba, E., Santoro, J., Rico, M., and Jimenez, M.A. (1999). De novo design of a monomeric three-stranded antiparallel β-sheet. Protein Sci. 8, 854-865.
    • (1999) Protein Sci. , vol.8 , pp. 854-865
    • De Alba, E.1    Santoro, J.2    Rico, M.3    Jimenez, M.A.4
  • 17
    • 0022098302 scopus 로고
    • Kinetics of collapse for a flexible coil
    • de Gennes, P.G. (1985). Kinetics of collapse for a flexible coil. J. Phys. Lett. 46, L639-L642.
    • (1985) J. Phys. Lett. , vol.46
    • De Gennes, P.G.1
  • 18
    • 0001931668 scopus 로고
    • Unfolded proteins, compact states and molten globules
    • Dobson, C.M. (1992). Unfolded proteins, compact states and molten globules. Curr. Opin. Struct. Biol. 2, 6-12.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 6-12
    • Dobson, C.M.1
  • 19
    • 84979113075 scopus 로고
    • Eine neue Bestimmung der Moleküldimensionen
    • Einstein, A. (1906). Eine neue Bestimmung der Moleküldimensionen. Ann. d. Phys. 19, 289-306.
    • (1906) Ann. D. Phys. , vol.19 , pp. 289-306
    • Einstein, A.1
  • 20
    • 0023490119 scopus 로고
    • Brownian dynamics of chain polymers
    • Fixman, M. (1987). Brownian dynamics of chain polymers. Farady Discuss. Chem. Soc. 83, 199-211.
    • (1987) Farady Discuss. Chem. Soc. , vol.83 , pp. 199-211
    • Fixman, M.1
  • 21
    • 0018368942 scopus 로고
    • Kinetics of the helix-coil transition of a polypeptide with non-ionic side chain groups, derived from ultrasonic relaxation measurements
    • Gruenewald, B., Nicola, C.U., Lustig, A., and Schwarz, G. (1979). Kinetics of the helix-coil transition of a polypeptide with non-ionic side chain groups, derived from ultrasonic relaxation measurements. Biopys. Chem. 9, 137-147.
    • (1979) Biopys. Chem. , vol.9 , pp. 137-147
    • Gruenewald, B.1    Nicola, C.U.2    Lustig, A.3    Schwarz, G.4
  • 22
    • 0029010695 scopus 로고
    • Kinetics of protein folding: Nucleation mechanism, time scales, and pathways
    • Guo, Z., and Thirumalai, D. (1995). Kinetics of protein folding: nucleation mechanism, time scales, and pathways. Biopolymers 36, 83-102.
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.1    Thirumalai, D.2
  • 23
    • 0017875133 scopus 로고
    • Brownian motion at the ends of oligopeptid chains as estimated by energy transfer between chain ends
    • Haas, E., Katchalski-Katzir, E., and Steinberg, I.Z. (1978). Brownian motion at the ends of oligopeptid chains as estimated by energy transfer between chain ends. Biopolymers 17, 11-31.
    • (1978) Biopolymers , vol.17 , pp. 11-31
    • Haas, E.1    Katchalski-Katzir, E.2    Steinberg, I.Z.3
  • 24
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding
    • Hagen, S.J., Hofrichter, J., Szabo, A., and Eaton, W.A. (1996). Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding. Proc. Natl. Acad. Sci. USA 93, 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
  • 25
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric λ repressor
    • Huang, G.S., and Oas, T.G. (1995). Submillisecond folding of monomeric λ repressor. Proc. Natl. Acad. Sci. USA 92, 6878-6882.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 26
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson, S.E., and Fersht, A.R. (1991). Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30, 10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 28
    • 3843114319 scopus 로고
    • Intramolecular reaction in polycondensations. I. The theory of linear systems
    • Jacobsen, H., and Stockmayer, W.H. (1950). Intramolecular reaction in polycondensations. I. The theory of linear systems. J. Phys. Chem. 18, 1600-1606.
    • (1950) J. Phys. Chem. , vol.18 , pp. 1600-1606
    • Jacobsen, H.1    Stockmayer, W.H.2
  • 29
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke, R. (1987). Folding and association of proteins. Progr. Biophys. Mol. Biol. 49, 117-237.
    • (1987) Progr. Biophys. Mol. Biol. , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 30
    • 0033042555 scopus 로고    scopus 로고
    • Stability and folding of domain proteins
    • Jaenicke, R. (1999). Stability and folding of domain proteins. Progr. Biophys. Mol. Biol. 71, 155-241.
    • (1999) Progr. Biophys. Mol. Biol. , vol.71 , pp. 155-241
    • Jaenicke, R.1
  • 32
    • 0025195732 scopus 로고
    • Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions
    • Kiefhaber, T., Quaas, R., Hahn, U., and Schmid, F.X. (1990). Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions. Biochemistry 29, 3061-3070.
    • (1990) Biochemistry , vol.29 , pp. 3061-3070
    • Kiefhaber, T.1    Quaas, R.2    Hahn, U.3    Schmid, F.X.4
  • 33
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P.S., and Baldwin, R.L. (1982). Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51, 459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 34
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S., and Baldwin, R.L. (1990). Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 35
    • 0022981913 scopus 로고
    • Loops in globular proteins: A novel category of secondary structure
    • Leszcynski, J.F., and Rose, J.D. (1986). Loops in globular proteins: a novel category of secondary structure. Science 234, 849-855.
    • (1986) Science , vol.234 , pp. 849-855
    • Leszcynski, J.F.1    Rose, J.D.2
  • 36
    • 0000333671 scopus 로고
    • On the theory of helix-coil transitions in polypeptides
    • Lifson, S., and Roig, A. (1961). On the theory of helix-coil transitions in polypeptides. J. Chem. Phys. 34, 1963-1974.
    • (1961) J. Chem. Phys. , vol.34 , pp. 1963-1974
    • Lifson, S.1    Roig, A.2
  • 37
    • 0027119143 scopus 로고
    • Internal stark effect measurement of the electric field at the amino terminus of an α-helix
    • Lockhart, D.J., and Kim, P.S. (1992). Internal stark effect measurement of the electric field at the amino terminus of an α-helix. Science 257, 947-951.
    • (1992) Science , vol.257 , pp. 947-951
    • Lockhart, D.J.1    Kim, P.S.2
  • 38
    • 0002830680 scopus 로고
    • Random coil configurations of polypeptide chains
    • Miller, W.G., Brant, D.A., and Flory, P.J. (1967). Random coil configurations of polypeptide chains. J. Mol. Biol. 23, 67-80.
    • (1967) J. Mol. Biol. , vol.23 , pp. 67-80
    • Miller, W.G.1    Brant, D.A.2    Flory, P.J.3
  • 39
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • Muñoz, V., Thompson, P., Hofrichter, J., and Eaton, W. (1997). Folding dynamics and mechanism of β-hairpin formation. Nature 390, 196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Muñoz, V.1    Thompson, P.2    Hofrichter, J.3    Eaton, W.4
  • 40
    • 0000227308 scopus 로고    scopus 로고
    • Variational theory for site resolved protein folding free energy surfaces
    • Portman, J.J., Takada, S., and Wolynes, P.G. (1998). Variational theory for site resolved protein folding free energy surfaces. Phys. Rev. Lett. 81, 5237-5240.
    • (1998) Phys. Rev. Lett. , vol.81 , pp. 5237-5240
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 42
    • 0026568185 scopus 로고
    • Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation
    • Rohl, C.A., Scholtz, J.M., York, E.J., Stewart, J.M., and Baldwin, R.L. (1992). Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation. Biochemistry 31, 1263-1269.
    • (1992) Biochemistry , vol.31 , pp. 1263-1269
    • Rohl, C.A.1    Scholtz, J.M.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 43
    • 33947476272 scopus 로고
    • The factors affecting the stability of hydrogen-bonded polypeptide structures in solution
    • Schellman, J.A. (1958). The factors affecting the stability of hydrogen-bonded polypeptide structures in solution. J. Phys. Chem. 62, 1485-1494.
    • (1958) J. Phys. Chem. , vol.62 , pp. 1485-1494
    • Schellman, J.A.1
  • 46
    • 0038933138 scopus 로고    scopus 로고
    • Folding of the disulfide-bonded β-sheet protein tendamistat: Rapid two-state folding without hydrophobic collapse
    • Schönbrunner, N., Koller, K.-P., and Kiefhaber, T. (1997). Folding of the disulfide-bonded β-sheet protein tendamistat: Rapid two-state folding without hydrophobic collapse. J. Mol. Biol. 268, 526-538.
    • (1997) J. Mol. Biol. , vol.268 , pp. 526-538
    • Schönbrunner, N.1    Koller, K.-P.2    Kiefhaber, T.3
  • 47
    • 78651171134 scopus 로고
    • On the kinetics of the helix-coil transition of polypeptides in solution
    • Schwarz, G. (1965). On the kinetics of the helix-coil transition of polypeptides in solution. J. Mol. Biol. 11, 64-77.
    • (1965) J. Mol. Biol. , vol.11 , pp. 64-77
    • Schwarz, G.1
  • 48
    • 0033532201 scopus 로고    scopus 로고
    • Characterization of transient intermediates in lysozyme folding with time-resolved small angle X-ray scattering
    • Segel, D., Bachmann, A., Hofrichter, J., Hodgson, K., Doniach, S., and Kiefhaber, T. (1999). Characterization of transient intermediates in lysozyme folding with time-resolved small angle X-ray scattering. J. Mol. Biol. 288, 489-500.
    • (1999) J. Mol. Biol. , vol.288 , pp. 489-500
    • Segel, D.1    Bachmann, A.2    Hofrichter, J.3    Hodgson, K.4    Doniach, S.5    Kiefhaber, T.6
  • 49
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond time scale
    • Shastry, M.C.R., and Roder, H. (1998). Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nat. Struct. Biol. 5, 385-392.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.R.1    Roder, H.2
  • 50
    • 36749116443 scopus 로고
    • First passage time approach to diffussion controlled reactions
    • Szabo, A., Schulten, K., and Schulten, Z. (1985). First passage time approach to diffussion controlled reactions. J. Chem. Phys. 72, 4350-4357.
    • (1985) J. Chem. Phys. , vol.72 , pp. 4350-4357
    • Szabo, A.1    Schulten, K.2    Schulten, Z.3
  • 52
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. (1968). Protein denaturation. Advan. Prot. Chem. 23, 121-282.
    • (1968) Advan. Prot. Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 54
    • 0000050196 scopus 로고
    • From minimal models to real protein: Time scales for protein folding kinetics
    • Thirumalai, D. (1995). From minimal models to real protein: time scales for protein folding kinetics. J. Phys. 5, 1457-1467.
    • (1995) J. Phys. , vol.5 , pp. 1457-1467
    • Thirumalai, D.1
  • 55
    • 0030789351 scopus 로고    scopus 로고
    • Laser temperature jump study of the helix-coil kinetics of an alanine peptide interpreted with a "kinetic zipper" model
    • Thompson, P., Eaton, W., and Hofrichter, J. (1997). Laser temperature jump study of the helix-coil kinetics of an alanine peptide interpreted with a "kinetic zipper" model. Biochemistry 36, 9200-9210.
    • (1997) Biochemistry , vol.36 , pp. 9200-9210
    • Thompson, P.1    Eaton, W.2    Hofrichter, J.3
  • 56
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition
    • Viguera, A.R., Martínez, J.C., Filimonov, V.V., Mateo, P.L., and Serrano, L. (1994). Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry 33, 2142.
    • (1994) Biochemistry , vol.33 , pp. 2142
    • Viguera, A.R.1    Martínez, J.C.2    Filimonov, V.V.3    Mateo, P.L.4    Serrano, L.5
  • 57
    • 84978694892 scopus 로고
    • Zur kinetischen Theorie der Brownschen Molekularbewegung und der Suspensionen
    • von Smoluchowski, M. (1906). Zur kinetischen Theorie der Brownschen Molekularbewegung und der Suspensionen. Ann. d. Phys. 21, 756-780.
    • (1906) Ann. D. Phys. , vol.21 , pp. 756-780
    • Von Smoluchowski, M.1
  • 58
    • 0001138912 scopus 로고
    • Drei Vorträge über Diffusion, Brownsche Molekularbewegung und Koagulation von Kolloidteilchen
    • von Smoluchowski, M. (1916). Drei Vorträge über Diffusion, Brownsche Molekularbewegung und Koagulation von Kolloidteilchen. Phys. Z. 17, 557-571.
    • (1916) Phys. Z. , vol.17 , pp. 557-571
    • Von Smoluchowski, M.1
  • 59
    • 0015305508 scopus 로고
    • Dielectric dispersion of the α-helix at the transition region to random coil
    • Wada, A., Tanaka, T., and Kihara, H. (1972). Dielectric dispersion of the α-helix at the transition region to random coil. Biopolymers 11, 587-605.
    • (1972) Biopolymers , vol.11 , pp. 587-605
    • Wada, A.1    Tanaka, T.2    Kihara, H.3
  • 61
    • 0024279235 scopus 로고
    • Analysis and prediction of the different types of β-turns in proteins
    • Wilmot, C.M., and Thornton, J.M. (1988). Analysis and prediction of the different types of β-turns in proteins. J. Mol. Biol. 203, 221-232.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 63
    • 0021754330 scopus 로고
    • Isolation, physicochemical properties, and folding of octopine dehydrogenase from Pecten jacobaeus
    • Zettlmeissl, G., Teschner, W., Rudolph, R., Jaenicke, R., and Gade, G. (1984). Isolation, physicochemical properties, and folding of octopine dehydrogenase from Pecten jacobaeus. Eur. J. Biochem. 143, 401-407.
    • (1984) Eur. J. Biochem. , vol.143 , pp. 401-407
    • Zettlmeissl, G.1    Teschner, W.2    Rudolph, R.3    Jaenicke, R.4    Gade, G.5
  • 64
    • 0000668407 scopus 로고
    • Theory of phase transition between helix and random coil in polypeptide chains
    • Zimm, B.H. and Bragg, J.K. (1959). Theory of phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31, 526-535.
    • (1959) J. Chem. Phys. , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.K.2


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