메뉴 건너뛰기




Volumn 44, Issue 17, 2005, Pages 6433-6439

Scanning malleable transition state ensembles: Comparing theory and experiment for folding protein U1A

Author keywords

[No Author keywords available]

Indexed keywords

FREE ENERGY; THERMAL EFFECTS;

EID: 17844377028     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0500170     Document Type: Article
Times cited : (31)

References (23)
  • 1
    • 0038329308 scopus 로고    scopus 로고
    • Folding at the speed limit
    • Yang, W. Y., and Gruebele, M. (2003) Folding at the speed limit, Nature 423, 193-196.
    • (2003) Nature , vol.423 , pp. 193-196
    • Yang, W.Y.1    Gruebele, M.2
  • 2
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • Sánchez, I. E., and Kiefhaber, T. (2003) Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding, J. Mol. Biol. 325, 367-376.
    • (2003) J. Mol. Biol. , vol.325 , pp. 367-376
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 5
    • 2342449128 scopus 로고    scopus 로고
    • Protein folding funnels: A kinetic approach to the sequence-structure relationship
    • Sato, S., Religa, T. L., Daggett, V., and Fersht, A. R. (2004) Protein folding funnels: A kinetic approach to the sequence-structure relationship, Proc. Natl. Acad. Sci. U.S.A. 101, 6952-6956.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 6952-6956
    • Sato, S.1    Religa, T.L.2    Daggett, V.3    Fersht, A.R.4
  • 6
    • 2342525803 scopus 로고    scopus 로고
    • Latest folding game results: Protein A barely frustrates computationalists
    • Wolynes, P. G. (2004) Latest folding game results: Protein A barely frustrates computationalists, Proc. Natl. Acad. Sci. U.S.A. 101, 6837-6838.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 6837-6838
    • Wolynes, P.G.1
  • 7
    • 0037418635 scopus 로고    scopus 로고
    • Hammond behavior versus ground-state effects in protein folding: Evidence for narrow free energy barriers and residual structure in unfolded states
    • Sánchez, I. E., and Kiefhaber, T. (2003) Hammond behavior versus ground-state effects in protein folding: Evidence for narrow free energy barriers and residual structure in unfolded states, J. Mol. Biol. 327, 867-884.
    • (2003) J. Mol. Biol. , vol.327 , pp. 867-884
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 8
    • 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
  • 9
    • 0035868476 scopus 로고    scopus 로고
    • Microscopic theory of protein folding rates. I. Fine structure of the free energy profile and folding routes from a variational approach
    • Portman, J. J., Takada, S., and Wolynes, P. G. (2001) Microscopic theory of protein folding rates. I. Fine structure of the free energy profile and folding routes from a variational approach, J. Chem. Phys. 114, 5069-5081.
    • (2001) J. Chem. Phys. , vol.114 , pp. 5069-5081
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 10
    • 0035868526 scopus 로고    scopus 로고
    • Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics
    • Portman, J. J., Takada, S., and Wolynes, P. G. (2001) Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics, J. Chem. Phys. 114, 5082-5096.
    • (2001) J. Chem. Phys. , vol.114 , pp. 5082-5096
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 11
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Gō, N. (1983) Theoretical studies of protein folding, Annu. Rev. Biophys. Bioeng. 12, 183-210.
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 183-210
    • Go, N.1
  • 12
    • 0026723063 scopus 로고
    • Protein folding funnels: A kinetic approach to the sequence-structure relationship
    • Leopold, P. E., Montal, M., and Onuchic, J. N. (1992) Protein folding funnels: A kinetic approach to the sequence-structure relationship, Proc. Natl. Acad. Sci. U.S.A. 89, 8721-8725.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 13
  • 14
    • 0037117477 scopus 로고    scopus 로고
    • Unspecific hydrophobic stabilization of folding transition states
    • Viguera, A. R., Vega, C., and Serrano, L. (2002) Unspecific hydrophobic stabilization of folding transition states. Proc. Natl. Acad. Sci. U.S.A. 99, 5349-5354.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5349-5354
    • Viguera, A.R.1    Vega, C.2    Serrano, L.3
  • 15
    • 0035826032 scopus 로고    scopus 로고
    • Role of explicitly cooperative interactions in protein folding funnels: A simulation study
    • Eastwood, M. P., and Wolynes, P. G. (2001) Role of explicitly cooperative interactions in protein folding funnels: A simulation study, J. Chem. Phys 114, 4702-4716.
    • (2001) J. Chem. Phys. , vol.114 , pp. 4702-4716
    • Eastwood, M.P.1    Wolynes, P.G.2
  • 16
    • 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. (2001) Characterisation of the transition states for protein folding: Towards a new level of mechanistic detail in protein engineering analysis, Curr. Opin. Struct. Biol. 11, 94-100.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 94-100
    • Oliveberg, M.1
  • 17
    • 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
    • Otzen, D. E., and Oliveberg, M. (2002) 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, 613-627.
    • (2002) J. Mol. Biol. , vol.317 , pp. 613-627
    • Otzen, D.E.1    Oliveberg, M.2
  • 18
    • 0032514483 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal U2B″-U2A′ protein complex bound to a fragment of U2 small nuclear RNA
    • Price, S., Evans, P. R., and Nagai, K. (1998) Crystal structure of the spliceosomal U2B″-U2A′ protein complex bound to a fragment of U2 small nuclear RNA, Nature 394, 645-650.
    • (1998) Nature , vol.394 , pp. 645-650
    • Price, S.1    Evans, P.R.2    Nagai, K.3
  • 19
    • 0029920331 scopus 로고    scopus 로고
    • Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation
    • Allain, F. H.-T., Gubser, C. C., Howe, P. W. A., Nagai, K., Neuhaus, D., and Varani, G. (1996) Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation, Nature 380, 646-650.
    • (1996) Nature , vol.380 , pp. 646-650
    • Allain, F.H.-T.1    Gubser, C.C.2    Howe, P.W.A.3    Nagai, K.4    Neuhaus, D.5    Varani, G.6
  • 20
    • 0030958760 scopus 로고    scopus 로고
    • Transient aggregates in protein folding are easily mistaken for folding intermediates
    • Silow, M., and Oliveberg, M. (1997) Transient aggregates in protein folding are easily mistaken for folding intermediates, Proc. Natl. Acad. Sci. U.S.A. 94, 6084-6086.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6084-6086
    • Silow, M.1    Oliveberg, M.2
  • 21
    • 0030750236 scopus 로고    scopus 로고
    • High-energy channeling in protein folding
    • Silow, M., and Oliveberg, M. (1997) High-energy channeling in protein folding, Biochemistry 36, 7633-7637.
    • (1997) Biochemistry , vol.36 , pp. 7633-7637
    • Silow, M.1    Oliveberg, M.2
  • 22
    • 0033592876 scopus 로고    scopus 로고
    • From snapshot to movie: Phi analysis of protein folding transition states taken one step further
    • Ternström, T., Mayor, U., Akke, M., and Oliveberg, M. (1999) From snapshot to movie: phi analysis of protein folding transition states taken one step further, Proc. Natl. Acad. Sci. U.S.A. 96, 14854-14859.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14854-14859
    • Ternström, T.1    Mayor, U.2    Akke, M.3    Oliveberg, M.4
  • 23
    • 0030979740 scopus 로고    scopus 로고
    • Folding funnels and energy landscapes of larger proteins within the capillarity approximation
    • Wolynes, P. G. (1997) Folding funnels and energy landscapes of larger proteins within the capillarity approximation, Proc. Natl. Acad. Sci. U.S.A. 94, 6170-6175.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6170-6175
    • Wolynes, P.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.