메뉴 건너뛰기




Volumn 397, Issue 3, 2010, Pages 789-798

A Survey of λ Repressor Fragments from Two-State to Downhill Folding

Author keywords

CD; cold denaturation; fluorescence; heat denaturation; temperature jump

Indexed keywords

MUTANT PROTEIN;

EID: 77649340195     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.01.071     Document Type: Article
Times cited : (31)

References (47)
  • 2
    • 0032989351 scopus 로고    scopus 로고
    • Observation of strange kinetics in protein folding
    • Sabelko J., Ervin J., and Gruebele M. Observation of strange kinetics in protein folding. Proc. Natl Acad. Sci. USA 96 (1999) 6031-6036
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6031-6036
    • Sabelko, J.1    Ervin, J.2    Gruebele, M.3
  • 3
    • 8644232674 scopus 로고    scopus 로고
    • A similarity measure for partially folded proteins: application to unfolded and native-like conformational fluctuations
    • Larios E., Yang W.Y., Schulten K., and Gruebele M. A similarity measure for partially folded proteins: application to unfolded and native-like conformational fluctuations. Chem. Phys. 307 (2004) 217-225
    • (2004) Chem. Phys. , vol.307 , pp. 217-225
    • Larios, E.1    Yang, W.Y.2    Schulten, K.3    Gruebele, M.4
  • 5
    • 29844443394 scopus 로고    scopus 로고
    • Direct measurement of barrier heights in protein folding
    • Naganathan A.N., Sanchez-Ruiz J.M., and Munoz V. Direct measurement of barrier heights in protein folding. J. Am. Chem. Soc. 127 (2005) 17970-17971
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17970-17971
    • Naganathan, A.N.1    Sanchez-Ruiz, J.M.2    Munoz, V.3
  • 6
    • 0015220649 scopus 로고
    • Kinetic evidence for incorrectly folded intermediate states in the refolding of denatured proteins
    • Ikai A., and Tanford C. Kinetic evidence for incorrectly folded intermediate states in the refolding of denatured proteins. Nature 230 (1971) 100-102
    • (1971) Nature , vol.230 , pp. 100-102
    • Ikai, A.1    Tanford, C.2
  • 7
    • 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. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51 (1982) 459-489
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 9
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric λ repressor
    • Huang G.S., and Oas T.G. Submillisecond folding of monomeric λ repressor. Proc. Natl Acad. Sci. USA 92 (1995) 6878-6882
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 10
    • 0029934661 scopus 로고    scopus 로고
    • Heat and cold denatured states of monomeric N repressor are thermodynamically and conformationally equivalent
    • Huang G.S., and Oas T.G. Heat and cold denatured states of monomeric N repressor are thermodynamically and conformationally equivalent. Biochemistry 35 (1996) 6173-6180
    • (1996) Biochemistry , vol.35 , pp. 6173-6180
    • Huang, G.S.1    Oas, T.G.2
  • 12
    • 0032554626 scopus 로고    scopus 로고
    • Protein folding dynamics: quantitative comparison between theory and experiment
    • Burton R.E., Myers J.K., and Oas T.G. Protein folding dynamics: quantitative comparison between theory and experiment. Biochemistry 37 (1998) 5337-5343
    • (1998) Biochemistry , vol.37 , pp. 5337-5343
    • Burton, R.E.1    Myers, J.K.2    Oas, T.G.3
  • 14
    • 0033602841 scopus 로고    scopus 로고
    • Contribution of a buried hydrogen bond to lambda repressor folding kinetics
    • Myers J.K., and Oas T.G. Contribution of a buried hydrogen bond to lambda repressor folding kinetics. Biochemistry 38 (1999) 6761-6768
    • (1999) Biochemistry , vol.38 , pp. 6761-6768
    • Myers, J.K.1    Oas, T.G.2
  • 16
    • 34250161638 scopus 로고    scopus 로고
    • Tuning λ6-85 towards downhill folding at its melting temperature
    • Liu F., and Gruebele M. Tuning λ6-85 towards downhill folding at its melting temperature. J. Mol. Biol. 370 (2007) 574-584
    • (2007) J. Mol. Biol. , vol.370 , pp. 574-584
    • Liu, F.1    Gruebele, M.2
  • 18
    • 14044258768 scopus 로고    scopus 로고
    • Kinetics are probe-dependent during downhill folding of an engineered lambda-6-85 protein
    • Ma H., and Gruebele M. Kinetics are probe-dependent during downhill folding of an engineered lambda-6-85 protein. Proc. Natl Acad. Sci. USA 102 (2005) 2283-2287
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 2283-2287
    • Ma, H.1    Gruebele, M.2
  • 19
    • 5444267817 scopus 로고    scopus 로고
    • Rate-temperature relationships in lambda repressor fragment 6-85 folding
    • Yang W.Y., and Gruebele M. Rate-temperature relationships in lambda repressor fragment 6-85 folding. Biochemistry 43 (2004) 13018-13025
    • (2004) Biochemistry , vol.43 , pp. 13018-13025
    • Yang, W.Y.1    Gruebele, M.2
  • 20
    • 3042814557 scopus 로고    scopus 로고
    • Folding lambda repressor at its speed limit
    • Yang W., and Gruebele M. Folding lambda repressor at its speed limit. Biophys. J. 87 (2004) 596-608
    • (2004) Biophys. J. , vol.87 , pp. 596-608
    • Yang, W.1    Gruebele, M.2
  • 21
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • Yang W.Y., and Gruebele M. Folding at the speed limit. Nature 423 (2003) 193-197
    • (2003) Nature , vol.423 , pp. 193-197
    • Yang, W.Y.1    Gruebele, M.2
  • 23
    • 0028147533 scopus 로고
    • The crystal structure of a mutant protein with altered but improved hydrophobic core packing
    • Lim W.A., Hodel A., Sauer R.T., and Richards F.M. The crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proc. Natl Acad. Sci. USA 91 (1994) 423-427
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 423-427
    • Lim, W.A.1    Hodel, A.2    Sauer, R.T.3    Richards, F.M.4
  • 25
    • 40649128566 scopus 로고    scopus 로고
    • An experimental survey of the transition between two-state and downhill protein folding scenarios
    • Liu F., Du D., Fuller A.A., Davoren J., Wipf P., Kelly J., and Gruebele M. An experimental survey of the transition between two-state and downhill protein folding scenarios. Proc. Natl Acad. Sci. USA 105 (2008) 2369-2374
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 2369-2374
    • Liu, F.1    Du, D.2    Fuller, A.A.3    Davoren, J.4    Wipf, P.5    Kelly, J.6    Gruebele, M.7
  • 26
    • 0035005366 scopus 로고    scopus 로고
    • Preorganized secondary structure as an important determinant of fast protein folding
    • Myers J.K., and Oas T.G. Preorganized secondary structure as an important determinant of fast protein folding. Nat. Struct. Biol. 8 (2001) 552-558
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 552-558
    • Myers, J.K.1    Oas, T.G.2
  • 27
    • 0028935887 scopus 로고
    • Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding
    • Huang G.S., and Oas T.G. Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding. Biochemistry 34 (1995) 3884-3892
    • (1995) Biochemistry , vol.34 , pp. 3884-3892
    • Huang, G.S.1    Oas, T.G.2
  • 28
    • 70450235210 scopus 로고    scopus 로고
    • The transition state transit time of WW domain folding is controlled by energy landscape roughness
    • Liu F., and Gruebele M. The transition state transit time of WW domain folding is controlled by energy landscape roughness. J. Chem. Phys. 131 (2009) 195101
    • (2009) J. Chem. Phys. , vol.131 , pp. 195101
    • Liu, F.1    Gruebele, M.2
  • 29
    • 0029040449 scopus 로고
    • Thermodynamic stability of the molten globule states of apomyoglobin
    • Nishii I., Kataoka M., and Goto Y. Thermodynamic stability of the molten globule states of apomyoglobin. J. Mol. Biol. 250 (1995) 223-238
    • (1995) J. Mol. Biol. , vol.250 , pp. 223-238
    • Nishii, I.1    Kataoka, M.2    Goto, Y.3
  • 31
    • 0026657433 scopus 로고
    • Refined 1.8 Å crystal structure of the lambda repressor-operator complex
    • Beamer L.J., and Pabo C.O. Refined 1.8 Å crystal structure of the lambda repressor-operator complex. J. Mol. Biol. 227 (1992) 177-196
    • (1992) J. Mol. Biol. , vol.227 , pp. 177-196
    • Beamer, L.J.1    Pabo, C.O.2
  • 32
    • 33749442647 scopus 로고    scopus 로고
    • MultiSeq: unifying sequence and structure data for evolutionary analysis
    • Roberts E., Eargle J., Wright D., and Luthey-Schulten Z. MultiSeq: unifying sequence and structure data for evolutionary analysis. BMC Bioinf. 7 (2006) 382
    • (2006) BMC Bioinf. , vol.7 , pp. 382
    • Roberts, E.1    Eargle, J.2    Wright, D.3    Luthey-Schulten, Z.4
  • 33
    • 84964589206 scopus 로고
    • Interferenz von Röntgenstrahlen und Wärmebewegung
    • Debye P. Interferenz von Röntgenstrahlen und Wärmebewegung. Ann. Phys. 348 (1913) 49-92
    • (1913) Ann. Phys. , vol.348 , pp. 49-92
    • Debye, P.1
  • 34
    • 84990647020 scopus 로고
    • The Debye-Waller factor: from villain to hero in protein crsytallography
    • Frauenfelder H. The Debye-Waller factor: from villain to hero in protein crsytallography. Int. J. Quantum Chem. 35 (1989) 711-715
    • (1989) Int. J. Quantum Chem. , vol.35 , pp. 711-715
    • Frauenfelder, H.1
  • 35
    • 33645406561 scopus 로고    scopus 로고
    • Correlation of early orientational ordering of engineered λ6-85 structure with kinetics and thermodynamics
    • Larios E., Pitera J.W., Swope W.C., and Gruebele M. Correlation of early orientational ordering of engineered λ6-85 structure with kinetics and thermodynamics. Chem. Phys. 323 (2006) 45-53
    • (2006) Chem. Phys. , vol.323 , pp. 45-53
    • Larios, E.1    Pitera, J.W.2    Swope, W.C.3    Gruebele, M.4
  • 36
    • 23944522022 scopus 로고    scopus 로고
    • Downhill protein folding: evolution meets physics
    • Gruebele M. Downhill protein folding: evolution meets physics. C. R. Biol. 328 (2005) 701-712
    • (2005) C. R. Biol. , vol.328 , pp. 701-712
    • Gruebele, M.1
  • 37
    • 0025908265 scopus 로고
    • The role of internal packing interactions in determining the structure and stability of a protein
    • Lim W.A., and Sauer R.T. The role of internal packing interactions in determining the structure and stability of a protein. J. Mol. Biol. 219 (1991) 359-376
    • (1991) J. Mol. Biol. , vol.219 , pp. 359-376
    • Lim, W.A.1    Sauer, R.T.2
  • 38
    • 0030992890 scopus 로고    scopus 로고
    • De novo design of the hydrophobic core of ubiquitin
    • Lazar G.A., Desjarlais J.R., and Handel T.M. De novo design of the hydrophobic core of ubiquitin. Protein Sci. 6 (1997) 1167-1178
    • (1997) Protein Sci. , vol.6 , pp. 1167-1178
    • Lazar, G.A.1    Desjarlais, J.R.2    Handel, T.M.3
  • 39
    • 44949091517 scopus 로고    scopus 로고
    • Expanding the realm of ultrafast protein folding: gpW, a midsize natural single-domain with alpha + beta topology that folds downhill
    • Fung A., Li P., Godoy-Ruiz R., Sanchez-Ruiz J.M., and Munoz V. Expanding the realm of ultrafast protein folding: gpW, a midsize natural single-domain with alpha + beta topology that folds downhill. J. Am. Chem. Soc. 130 (2008) 7489-7495
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 7489-7495
    • Fung, A.1    Li, P.2    Godoy-Ruiz, R.3    Sanchez-Ruiz, J.M.4    Munoz, V.5
  • 40
    • 38549129313 scopus 로고    scopus 로고
    • Comment on: Probe-dependent and nonexponential relaxation kinetics: unreliable signatures of downhill protein folding
    • Gruebele M. Comment on: Probe-dependent and nonexponential relaxation kinetics: unreliable signatures of downhill protein folding. Proteins Struct. Funct. Bioinf. 70 (2008) 1099-1102
    • (2008) Proteins Struct. Funct. Bioinf. , vol.70 , pp. 1099-1102
    • Gruebele, M.1
  • 42
    • 49349096539 scopus 로고    scopus 로고
    • Folding kinetics of a naturally occurring helical peptide: implication of the folding speed limit of helical proteins
    • Mukherjee S., Chowdhury P., Bunagan M.R., and Gai F. Folding kinetics of a naturally occurring helical peptide: implication of the folding speed limit of helical proteins. J. Phys. Chem. B 112 (2008) 9146-9150
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9146-9150
    • Mukherjee, S.1    Chowdhury, P.2    Bunagan, M.R.3    Gai, F.4
  • 43
    • 67749147584 scopus 로고    scopus 로고
    • Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories
    • Chung H.S., Louis J.M., and Eaton W.A. Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories. Proc. Natl Acad. Sci. USA 106 (2009) 11837-11844
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 11837-11844
    • Chung, H.S.1    Louis, J.M.2    Eaton, W.A.3
  • 44
    • 70350020368 scopus 로고    scopus 로고
    • Direct observation of downhill folding of lambda-repressor in a microfluidic mixer
    • DeCamp S.J., Naganathan A.N., Waldauer S.A., Bakajin O., and Lapidus L.J. Direct observation of downhill folding of lambda-repressor in a microfluidic mixer. Biophys. J. 97 (2009) 1772-1777
    • (2009) Biophys. J. , vol.97 , pp. 1772-1777
    • DeCamp, S.J.1    Naganathan, A.N.2    Waldauer, S.A.3    Bakajin, O.4    Lapidus, L.J.5
  • 45
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6 (1967) 1948-1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 46
    • 0033996482 scopus 로고    scopus 로고
    • Submicrosecond real-time fluorescence detection: application to protein folding
    • Ervin J., Sabelko J., and Gruebele M. Submicrosecond real-time fluorescence detection: application to protein folding. J. Photochem. Photobiol. B 54 (2000) 1-15
    • (2000) J. Photochem. Photobiol. B , vol.54 , pp. 1-15
    • Ervin, J.1    Sabelko, J.2    Gruebele, M.3
  • 47
    • 33751117974 scopus 로고    scopus 로고
    • Kinetic equivalence of the heat and cold structural transitions of lambda6-85
    • Yang W.Y., and Gruebele M. Kinetic equivalence of the heat and cold structural transitions of lambda6-85. Philos. Trans. R. Soc. London Ser. B 43 (2005) 13018-13025
    • (2005) Philos. Trans. R. Soc. London Ser. B , vol.43 , pp. 13018-13025
    • Yang, W.Y.1    Gruebele, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.