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Volumn 107, Issue 8, 2014, Pages 1997-1998

Only kinetics can prove conformational selection

Author keywords

[No Author keywords available]

Indexed keywords

INTRINSICALLY DISORDERED PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84908257600     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.08.037     Document Type: Editorial
Times cited : (13)

References (14)
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  • 2
    • 84857839467 scopus 로고    scopus 로고
    • Multiparametric analysis of intrinsically disordered proteins: Looking at intrinsic disorder through compound eyes
    • V.N. Uversky, and A.K. Dunker Multiparametric analysis of intrinsically disordered proteins: looking at intrinsic disorder through compound eyes Anal. Chem. 84 2012 2096 2104
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  • 3
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • M. Fuxreiter, and I. Simon P. Tompa Preformed structural elements feature in partner recognition by intrinsically unstructured proteins J. Mol. Biol. 338 2004 1015 1026
    • (2004) J. Mol. Biol. , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Tompa, P.3
  • 4
    • 84893454221 scopus 로고    scopus 로고
    • Helical propensity in an intrinsically disordered protein accelerates ligand binding
    • V. Iešmantavičius, and J. Dogan M. Kjaergaard Helical propensity in an intrinsically disordered protein accelerates ligand binding Angew. Chem. Int. Ed. Engl. 53 2014 1548 1551
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , pp. 1548-1551
    • Iešmantavičius, V.1    Dogan, J.2    Kjaergaard, M.3
  • 5
    • 84892983861 scopus 로고    scopus 로고
    • Ligand concentration regulates the pathways of coupled protein folding and binding
    • K.G. Daniels, and N.K. Tonthat T.G. Oas Ligand concentration regulates the pathways of coupled protein folding and binding J. Am. Chem. Soc. 136 2014 822 825
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 822-825
    • Daniels, K.G.1    Tonthat, N.K.2    Oas, T.G.3
  • 6
    • 84896336036 scopus 로고    scopus 로고
    • The binding mechanisms of intrinsically disordered proteins
    • J. Dogan, S. Gianni, and P. Jemth The binding mechanisms of intrinsically disordered proteins Phys. Chem. Chem. Phys. 16 2013 6323 6331
    • (2013) Phys. Chem. Chem. Phys. , vol.16 , pp. 6323-6331
    • Dogan, J.1    Gianni, S.2    Jemth, P.3
  • 7
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: A flux description of reaction mechanism
    • G.G. Hammes, Y.-C. Chang, and T.G. Oas Conformational selection or induced fit: a flux description of reaction mechanism Proc. Natl. Acad. Sci. USA 106 2009 13737 13741
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.-C.2    Oas, T.G.3
  • 8
    • 79952741171 scopus 로고    scopus 로고
    • Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction
    • A. Bachmann, and D. Wildemann T. Kiefhaber Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction Proc. Natl. Acad. Sci. USA 108 2011 3952 3957
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 3952-3957
    • Bachmann, A.1    Wildemann, D.2    Kiefhaber, T.3
  • 9
    • 84883780574 scopus 로고    scopus 로고
    • The transition state structure for coupled binding and folding of disordered protein domains
    • J. Dogan, and X. Mu P. Jemth The transition state structure for coupled binding and folding of disordered protein domains Sci. Rep 3 2013 2076
    • (2013) Sci. Rep , vol.3 , pp. 2076
    • Dogan, J.1    Mu, X.2    Jemth, P.3
  • 10
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    • Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system
    • R. Giri, and A. Morrone S. Gianni Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system Proc. Natl. Acad. Sci. USA 110 2013 14942 14947
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    • Giri, R.1    Morrone, A.2    Gianni, S.3
  • 11
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    • Coupled folding and binding of the disordered protein PUMA does not require particular residual structure
    • J.M. Rogers, C.T. Wong, and J. Clarke Coupled folding and binding of the disordered protein PUMA does not require particular residual structure J. Am. Chem. Soc. 136 2014 5197 5200
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 5197-5200
    • Rogers, J.M.1    Wong, C.T.2    Clarke, J.3
  • 12
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    • Gianni, S.1    Dogan, J.2    Jemth, P.3
  • 14
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    • Local conformational dynamics in α-helices measured by fast triplet transfer
    • B. Fierz, A. Reiner, and T. Kiefhaber Local conformational dynamics in α-helices measured by fast triplet transfer Proc. Natl. Acad. Sci. USA 106 2009 1057 1062
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    • Fierz, B.1    Reiner, A.2    Kiefhaber, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.