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Volumn 326, Issue 1, 2003, Pages 263-271

High concentrations of viscogens decrease the protein folding rate constant by prematurely collapsing the coil

Author keywords

Denatured state; Folding energy landscape; Protein engineering; Protein folding; Viscosity

Indexed keywords

CHYMOTRYPSIN INHIBITOR 2; ETHYLENE GLYCOL; MACROGOL; MACROGOL 200; MACROGOL 400; PROTEIN; SOLVENT; STABILIZING AGENT; SUCROSE; UNCLASSIFIED DRUG;

EID: 0037423748     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01331-1     Document Type: Article
Times cited : (33)

References (42)
  • 2
    • 0028838794 scopus 로고
    • Stabilizing effect of sucrose against irreversible denaturation of rabbit muscle lactate dehydrogenase
    • Hall D.R., Jacobsen M.P., Winzor D.J. Stabilizing effect of sucrose against irreversible denaturation of rabbit muscle lactate dehydrogenase. Biophys. Chem. 57:1995;47-54.
    • (1995) Biophys. Chem. , vol.57 , pp. 47-54
    • Hall, D.R.1    Jacobsen, M.P.2    Winzor, D.J.3
  • 3
    • 0022286246 scopus 로고
    • Use of polyethylene glycol in the crystallization of macromolecules
    • McPherson A. Use of polyethylene glycol in the crystallization of macromolecules. Methods Enzymol. 114:1985;120-125.
    • (1985) Methods Enzymol. , vol.114 , pp. 120-125
    • McPherson, A.1
  • 4
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff S.N. The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22:1993;67-97.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 6
    • 0032506017 scopus 로고    scopus 로고
    • Limited internal friction in the rate-limiting step of a two-state protein folding reaction
    • Plaxco K.W., Baker D. Limited internal friction in the rate-limiting step of a two-state protein folding reaction. Proc. Natl Acad. Sci. USA. 95:1998;13591-13596.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13591-13596
    • Plaxco, K.W.1    Baker, D.2
  • 7
    • 0025214083 scopus 로고
    • Role of diffusion in the folding of the alpha subunit of tryptophan synthase from Escherichia coli
    • Chrunyk B.A., Matthews C.R. Role of diffusion in the folding of the alpha subunit of tryptophan synthase from Escherichia coli. Biochemistry. 29:1990;2149-2154.
    • (1990) Biochemistry , vol.29 , pp. 2149-2154
    • Chrunyk, B.A.1    Matthews, C.R.2
  • 8
    • 0032562222 scopus 로고    scopus 로고
    • Kinetic mechanism of a partial folding reaction. 2. Nature of the transition state
    • Goldberg J.M., Baldwin R.L. Kinetic mechanism of a partial folding reaction. 2. Nature of the transition state. Biochemistry. 37:1998;2556-2563.
    • (1998) Biochemistry , vol.37 , pp. 2556-2563
    • Goldberg, J.M.1    Baldwin, R.L.2
  • 9
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
    • Waldburger C.D., Jonsson T., Sauer R.T. Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. Proc. Natl Acad. Sci. USA. 93:1996;2629-2634.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2629-2634
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 10
    • 0033596697 scopus 로고    scopus 로고
    • Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil
    • Bhattacharyya R.P., Sosnick T.R. Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. Biochemistry. 38:1999;2601-2609.
    • (1999) Biochemistry , vol.38 , pp. 2601-2609
    • Bhattacharyya, R.P.1    Sosnick, T.R.2
  • 11
    • 0032853084 scopus 로고    scopus 로고
    • Diffusional barrier crossing in a two-state protein folding reaction
    • Jacob M., Geeves M., Holtermann G., Schmid F.X. Diffusional barrier crossing in a two-state protein folding reaction. Nature Struct. Biol. 6:1999;923-926.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 923-926
    • Jacob, M.1    Geeves, M.2    Holtermann, G.3    Schmid, F.X.4
  • 12
    • 0033849085 scopus 로고    scopus 로고
    • The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding
    • Sato S., Sayid C.J., Raleigh D.P. The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding. Protein Sci. 9:2000;1601-1603.
    • (2000) Protein Sci. , vol.9 , pp. 1601-1603
    • Sato, S.1    Sayid, C.J.2    Raleigh, D.P.3
  • 13
    • 0032921819 scopus 로고    scopus 로고
    • Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2
    • Ladurner A.G., Fersht A.R. Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2. Nature Struct. Biol. 6:1999;28-31.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 28-31
    • Ladurner, A.G.1    Fersht, A.R.2
  • 14
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki L.S., Otzen D.E., Fersht A.R. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering: 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    Otzen, D.E.2    Fersht, A.R.3
  • 15
    • 0030450051 scopus 로고    scopus 로고
    • Thermodynamic properties of an extremely rapid protein folding reaction
    • Schindler T., Schmid F.X. Thermodynamic properties of an extremely rapid protein folding reaction. Biochemistry. 35:1996;16833-16842.
    • (1996) Biochemistry , vol.35 , pp. 16833-16842
    • Schindler, T.1    Schmid, F.X.2
  • 16
    • 0028944346 scopus 로고
    • Is burst hydrophobic collapse necessary for protein folding?
    • Gutin A.M., Abkevich V.I., Shakhnovich E.I. Is burst hydrophobic collapse necessary for protein folding? Biochemistry. 34:1995;3066-3076.
    • (1995) Biochemistry , vol.34 , pp. 3066-3076
    • Gutin, A.M.1    Abkevich, V.I.2    Shakhnovich, E.I.3
  • 17
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson S.E., Fersht A.R. 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
  • 18
    • 0032878322 scopus 로고    scopus 로고
    • Formation of short-lived protein aggregates directly from the coil in two-state folding
    • Silow M., Tan Y.J., Fersht A.R., Oliveberg M. Formation of short-lived protein aggregates directly from the coil in two-state folding. Biochemistry. 38:1999;13006-13012.
    • (1999) Biochemistry , vol.38 , pp. 13006-13012
    • Silow, M.1    Tan, Y.J.2    Fersht, A.R.3    Oliveberg, M.4
  • 19
    • 0031580205 scopus 로고    scopus 로고
    • The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2
    • Tan Y.J., Oliveberg M., Otzen D.E., Fersht A.R. The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2. J. Mol. Biol. 269:1997;611-622.
    • (1997) J. Mol. Biol. , vol.269 , pp. 611-622
    • Tan, Y.J.1    Oliveberg, M.2    Otzen, D.E.3    Fersht, A.R.4
  • 20
    • 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
  • 21
    • 0030606223 scopus 로고    scopus 로고
    • Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways
    • Tan Y.J., Oliveberg M., Fersht A.R. Titration properties and thermodynamics of the transition state for folding: comparison of two-state and multi-state 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
  • 22
    • 0000384736 scopus 로고    scopus 로고
    • Alternative explanations for multi-state kinetics in protein folding: Transient aggregation and changing transition-state ensembles
    • Oliveberg M. Alternative explanations for multi-state kinetics in protein folding: transient aggregation and changing transition-state ensembles. Acc. Chem. Res. 31:1998;765-772.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 765-772
    • Oliveberg, M.1
  • 23
    • 0030750236 scopus 로고    scopus 로고
    • High-energy channeling in protein folding
    • Silow M., Oliveberg M. High-energy channeling in protein folding. Biochemistry. 36:1997;7633-7637.
    • (1997) Biochemistry , vol.36 , pp. 7633-7637
    • Silow, M.1    Oliveberg, M.2
  • 24
    • 0035252685 scopus 로고    scopus 로고
    • Characterisation of the transition states for protein folding: Towards a new level of mechanistic detail in protein engineering analysis
    • Oliveberg M. 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
  • 25
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek A., Kellis J.T. Jr, Serrano L., Fersht A.R. 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
  • 26
    • 0036293485 scopus 로고    scopus 로고
    • Conformational plasticity in folding of the split β-α-β protein S6: Evidence for burst-phase disruption of the native state
    • Otzen D.E., Oliveberg M. Conformational plasticity in folding of the split β-α-β protein S6: evidence for burst-phase disruption of the native state. J. Mol. Biol. 317:2002;639-653.
    • (2002) J. Mol. Biol. , vol.317 , pp. 639-653
    • Otzen, D.E.1    Oliveberg, M.2
  • 27
    • 0019585856 scopus 로고
    • Preferential hydration of bovine serum albumin in polyhydric alcohol-water mixtures
    • Gekko K., Morikawa T. Preferential hydration of bovine serum albumin in polyhydric alcohol-water mixtures. J. Biochem. (Tokyo). 90:1981;39-50.
    • (1981) J. Biochem. (Tokyo) , vol.90 , pp. 39-50
    • Gekko, K.1    Morikawa, T.2
  • 28
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
    • Gekko K., Timasheff S.N. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry. 20:1981;4667-4676.
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 29
    • 0019872612 scopus 로고
    • Thermodynamic and kinetic examination of protein stabilization by glycerol
    • Gekko K., Timasheff S.N. Thermodynamic and kinetic examination of protein stabilization by glycerol. Biochemistry. 20:1981;4677-4686.
    • (1981) Biochemistry , vol.20 , pp. 4677-4686
    • Gekko, K.1    Timasheff, S.N.2
  • 30
    • 0025268101 scopus 로고
    • Competing solvent effects of polyols and guanidine hydrochloride on protein stability
    • Gekko K., Ito H. Competing solvent effects of polyols and guanidine hydrochloride on protein stability. J. Biochem. (Tokyo). 107:1990;572-577.
    • (1990) J. Biochem. (Tokyo) , vol.107 , pp. 572-577
    • Gekko, K.1    Ito, H.2
  • 31
    • 0019590230 scopus 로고
    • Thermodynamics of polyol-induced thermal stabilization of chymotrypsinogen
    • Gekko K., Morikawa T. Thermodynamics of polyol-induced thermal stabilization of chymotrypsinogen. J. Biochem. (Tokyo). 90:1981;51-60.
    • (1981) J. Biochem. (Tokyo) , vol.90 , pp. 51-60
    • Gekko, K.1    Morikawa, T.2
  • 32
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and diffusion model of chemical reactions
    • Kramers H.A. Brownian motion in a field of force and diffusion model of chemical reactions. Physica. 7:1940;284-304.
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 34
    • 0000823411 scopus 로고
    • Some possible relationships of carbohydrates and other biological components with the water structure at 37°
    • Warner D.T. Some possible relationships of carbohydrates and other biological components with the water structure at 37° Nature. 196:1962;1055-1058.
    • (1962) Nature , vol.196 , pp. 1055-1058
    • Warner, D.T.1
  • 35
    • 0000966076 scopus 로고
    • Quantum chemical conformational analysis of 1, 2-ethanediol: Correlation and solvation effects on the tendency to form internal hydrogen bonds in the gas phase and aqueous solution
    • Cramer C.J., Truhlar D.G. Quantum chemical conformational analysis of 1, 2-ethanediol: correlation and solvation effects on the tendency to form internal hydrogen bonds in the gas phase and aqueous solution. J. Am. Chem. Soc. 116:1994;3892-3900.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 3892-3900
    • Cramer, C.J.1    Truhlar, D.G.2
  • 36
    • 0032483027 scopus 로고    scopus 로고
    • Osmolyte-driven contraction of a random coil protein
    • Qu Y., Bolen C.L., Bolen D.W. Osmolyte-driven contraction of a random coil protein. Proc. Natl Acad. Sci. USA. 95:1998;9268-9273.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9268-9273
    • Qu, Y.1    Bolen, C.L.2    Bolen, D.W.3
  • 37
    • 1842298212 scopus 로고    scopus 로고
    • From levinthal to pathways to funnels
    • Dill K.A., Chan H.S. From levinthal to pathways to funnels. Nature Struct. Biol. 4:1997;10-19.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 38
    • 0032718386 scopus 로고    scopus 로고
    • Salt-induced detour through compact regions of the protein folding landscape
    • Otzen D.E., Oliveberg M. Salt-induced detour through compact regions of the protein folding landscape. Proc. Natl Acad. Sci. USA. 96:1999;11746-11751.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11746-11751
    • Otzen, D.E.1    Oliveberg, M.2
  • 39
    • 0033592876 scopus 로고    scopus 로고
    • From snapshot to movie: Phi analysis of protein folding transition states taken one step further
    • Ternstrom T., Mayor U., Akke M., Oliveberg M. 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
  • 40
    • 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., Eaton W.A. 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
  • 41
    • 0034612228 scopus 로고    scopus 로고
    • Investigation of routes and funnels in protein folding by free energy functional methods
    • Plotkin S.S., Onuchic J.N. Investigation of routes and funnels in protein folding by free energy functional methods. Proc. Natl Acad. Sci. USA. 97:2000;6509-6514.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6509-6514
    • Plotkin, S.S.1    Onuchic, J.N.2
  • 42
    • 0036829967 scopus 로고    scopus 로고
    • Complete change of the protein folding transition state upon circular permutation
    • Lindberg M.O., Tangrot J., Oliveberg M. Complete change of the protein folding transition state upon circular permutation. Nature Struct. Biol. 9:2002;818-822.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 818-822
    • Lindberg, M.O.1    Tangrot, J.2    Oliveberg, M.3


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