메뉴 건너뛰기




Volumn 405, Issue 1, 2011, Pages 43-48

Computational design and experimental testing of the fastest-folding β-sheet protein

Author keywords

fluorescence; molecular dynamics; protein engineering; temperature jump; WW domain

Indexed keywords

AMINO ACID; FIP35 PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 78650415889     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.10.023     Document Type: Article
Times cited : (100)

References (33)
  • 1
    • 0033624685 scopus 로고    scopus 로고
    • Fast kinetics and mechanisms in protein folding
    • Eaton W.A. Fast kinetics and mechanisms in protein folding Annu. Rev. Biophys. Biomol. Struct. 29 2000 327 359
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 327-359
    • Eaton, W.A.1
  • 2
    • 0030584652 scopus 로고    scopus 로고
    • Protein folding triggered by electron transfer
    • Pascher T., Chesick J.P., Winkler J.R., and Gray H.B. Protein folding triggered by electron transfer Science 271 1996 1558 1560
    • (1996) Science , vol.271 , pp. 1558-1560
    • Pascher, T.1    Chesick, J.P.2    Winkler, J.R.3    Gray, H.B.4
  • 3
    • 0037038372 scopus 로고    scopus 로고
    • Absolute comparison of simulated and experimental protein-folding dynamics
    • Snow C.D., Nguyen H., Pande V.S., and Gruebele M. Absolute comparison of simulated and experimental protein-folding dynamics Nature 420 2002 102 106
    • (2002) Nature , vol.420 , pp. 102-106
    • Snow, C.D.1    Nguyen, H.2    Pande, V.S.3    Gruebele, M.4
  • 4
    • 0037456298 scopus 로고    scopus 로고
    • The complete folding pathway of a protein from nanoseconds to microseconds
    • Mayor U. 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
  • 5
    • 33846917230 scopus 로고    scopus 로고
    • Ultrafast and downhill protein folding
    • Dyer R.B. Ultrafast and downhill protein folding Curr. Opin. Struct. Biol. 17 2007 38 47
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 38-47
    • Dyer, R.B.1
  • 6
    • 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
  • 9
    • 0035818471 scopus 로고    scopus 로고
    • Ultrafast folding of WW domains without structured aromatic clusters in the denatured state
    • Ferguson N. Ultrafast folding of WW domains without structured aromatic clusters in the denatured state Proc. Natl Acad. Sci. USA 98 2001 13002 13007
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 13002-13007
    • Ferguson, N.1
  • 10
    • 33746042979 scopus 로고    scopus 로고
    • Structure-function-folding relationship in a WW domain
    • Jager M. Structure-function-folding relationship in a WW domain Proc. Natl Acad. Sci. USA 103 2006 10648 10653
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 10648-10653
    • Jager, M.1
  • 11
    • 3042848873 scopus 로고    scopus 로고
    • Context-dependent contributions of backbone hydrogen bonding to β-sheet folding energetic
    • Deechongkit S. Context-dependent contributions of backbone hydrogen bonding to β-sheet folding energetic Nature 430 2004 101 105
    • (2004) Nature , vol.430 , pp. 101-105
    • Deechongkit, S.1
  • 12
    • 33745606942 scopus 로고    scopus 로고
    • Phi-analysis at the experimental limits: Mechanism of β-hairpin formation
    • Petrovich M., Jonsson A.L., Ferguson N., Daggett V., and Fersht A.R. Phi-analysis at the experimental limits: mechanism of β-hairpin formation J. Mol. Biol. 360 2006 865 881
    • (2006) J. Mol. Biol. , vol.360 , pp. 865-881
    • Petrovich, M.1    Jonsson, A.L.2    Ferguson, N.3    Daggett, V.4    Fersht, A.R.5
  • 13
    • 40649128566 scopus 로고    scopus 로고
    • An experimental survey of the transition between two-state and downhill protein folding scenarios
    • Liu F. 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
  • 14
    • 24344464777 scopus 로고    scopus 로고
    • Engineering a β-sheet protein toward the folding speed limit
    • Nguyen H., Jager M., Kelly J.W., and Gruebele M. Engineering a β-sheet protein toward the folding speed limit J. Phys. Chem. B 109 2005 15182 15186
    • (2005) J. Phys. Chem. B , vol.109 , pp. 15182-15186
    • Nguyen, H.1    Jager, M.2    Kelly, J.W.3    Gruebele, M.4
  • 15
    • 67650468079 scopus 로고    scopus 로고
    • Evaluating β-turn mimics as β-sheet folding nucleators
    • Fuller A.A. Evaluating β-turn mimics as β-sheet folding nucleators Proc. Natl Acad. Sci, USA 106 2009 11067 11072
    • (2009) Proc. Natl Acad. Sci, USA , vol.106 , pp. 11067-11072
    • Fuller, A.A.1
  • 18
    • 77957937199 scopus 로고    scopus 로고
    • Atomic-level characterization of the structural dynamics of proteins
    • Shaw D.E. Atomic-level characterization of the structural dynamics of proteins Science 330 2010 341 346
    • (2010) Science , vol.330 , pp. 341-346
    • Shaw, D.E.1
  • 20
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou P.Y., and Fasman G.D. Prediction of protein conformation Biochemistry 13 1974 222 245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 21
    • 70450235210 scopus 로고    scopus 로고
    • The transition state transit time of WW domain folding is controlled by energy landscape roughness
    • 195101
    • Liu F., Nakaema M., and Gruebele M. The transition state transit time of WW domain folding is controlled by energy landscape roughness J. Chem. Phys. 131 195101 2009
    • (2009) J. Chem. Phys. , vol.131
    • Liu, F.1    Nakaema, M.2    Gruebele, M.3
  • 22
    • 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
  • 23
    • 33845403686 scopus 로고    scopus 로고
    • Nanosecond folding dynamics of a three-stranded β-sheet
    • Xu Y., Purkayastha P., and Gai F. Nanosecond folding dynamics of a three-stranded β-sheet J. Am. Chem. Soc. 128 2006 15836 15842
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 15836-15842
    • Xu, Y.1    Purkayastha, P.2    Gai, F.3
  • 24
    • 0142185492 scopus 로고    scopus 로고
    • The denatured state of Engrailed Homeodomain under denaturing and native conditions
    • Mayor U., Grossmann J.G., Foster N.W., Freund S.M., and Fersht A.R. The denatured state of Engrailed Homeodomain under denaturing and native conditions J. Mol. Biol. 333 2003 977 991
    • (2003) J. Mol. Biol. , vol.333 , pp. 977-991
    • Mayor, U.1    Grossmann, J.G.2    Foster, N.W.3    Freund, S.M.4    Fersht, A.R.5
  • 25
    • 0345255608 scopus 로고    scopus 로고
    • Unifying features in protein-folding mechanisms
    • Gianni S. Unifying features in protein-folding mechanisms Proc. Natl Acad. Sci. USA 100 2003 13286 13291
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13286-13291
    • Gianni, S.1
  • 26
    • 76249117417 scopus 로고    scopus 로고
    • Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family
    • Wensley B.G. Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family Nature 463 2010 685 688
    • (2010) Nature , vol.463 , pp. 685-688
    • Wensley, B.G.1
  • 29
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force field
    • Lindorff-Larsen K. Improved side-chain torsion potentials for the Amber ff99SB protein force field Proteins 78 2010 1950 1958
    • (2010) Proteins , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1
  • 30
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • Hornak V., Abel R., Okur A., Strockbine B., Roitberg A., and Simmerling C. Comparison of multiple Amber force fields and development of improved protein backbone parameters Proteins 65 2006 712 725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 31
    • 0042561888 scopus 로고    scopus 로고
    • Solvent viscosity dependence of the folding rate of a small protein: Distributed computing study
    • Zagrovic B., and Pande V.S. Solvent viscosity dependence of the folding rate of a small protein: distributed computing study J. Comp. Chem. 24 2003 1432 1436
    • (2003) J. Comp. Chem. , vol.24 , pp. 1432-1436
    • Zagrovic, B.1    Pande, V.S.2
  • 32
    • 0029619259 scopus 로고
    • STRIDE: A web server for secondary structure assignment from known atomic coordinates of proteins
    • Frishman D., and Argos P. STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins Proteins 23 1995 566 579
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 33
    • 0029973119 scopus 로고    scopus 로고
    • Direct observation of fast protein folding: The initial collapse of apomyoglobin
    • Ballew R.M., Sabelko J., and Gruebele M. Direct observation of fast protein folding: the initial collapse of apomyoglobin Proc. Natl Acad. Sci. USA 93 1996 5759 5764
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5759-5764
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.