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Volumn 36, Issue , 2016, Pages 18-24

Coupled binding and folding of intrinsically disordered proteins: What can we learn from kinetics?

Author keywords

[No Author keywords available]

Indexed keywords

INTRINSICALLY DISORDERED PROTEIN; PROTEIN BINDING;

EID: 84959288285     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2015.11.012     Document Type: Review
Times cited : (76)

References (68)
  • 1
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity
    • Kriwacki R.W., Hengst L., Tennant L., Reed S.I., Wright P.E. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc Natl Acad Sci U S A 1996, 93:11504-11509.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 2
    • 0030980926 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28
    • Daughdrill G.W., Chadsey M.S., Karlinsey J.E., Hughes K.T., Dahlquist F.W. The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. Nat Struct Biol 1997, 4:285-291.
    • (1997) Nat Struct Biol , vol.4 , pp. 285-291
    • Daughdrill, G.W.1    Chadsey, M.S.2    Karlinsey, J.E.3    Hughes, K.T.4    Dahlquist, F.W.5
  • 3
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 1999, 293:321-331.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 4
    • 0034669882 scopus 로고    scopus 로고
    • Why are 'natively unfolded' proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., Fink A.L. Why are 'natively unfolded' proteins unstructured under physiologic conditions?. Proteins 2000, 41:415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 6
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: a point where biology waits for physics
    • Uversky V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci 2002, 11:739-756.
    • (2002) Protein Sci , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 7
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem Sci 2002, 27:527-533.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 8
    • 84857839467 scopus 로고    scopus 로고
    • Multiparametric analysis of intrinsically disordered proteins: looking at intrinsic disorder through compound eyes
    • Uversky V.N., Dunker A.K. Multiparametric analysis of intrinsically disordered proteins: looking at intrinsic disorder through compound eyes. Anal Chem 2012, 84:2096-2104.
    • (2012) Anal Chem , vol.84 , pp. 2096-2104
    • Uversky, V.N.1    Dunker, A.K.2
  • 9
    • 84883471917 scopus 로고    scopus 로고
    • From sequence and forces to structure, function, and evolution of intrinsically disordered proteins
    • Forman-Kay J.D., Mittag T. From sequence and forces to structure, function, and evolution of intrinsically disordered proteins. Structure 2013, 21:1492-1499.
    • (2013) Structure , vol.21 , pp. 1492-1499
    • Forman-Kay, J.D.1    Mittag, T.2
  • 10
    • 84903957091 scopus 로고    scopus 로고
    • Introducing protein intrinsic disorder
    • Habchi J., Tompa P., Longhi S., Uversky V.N. Introducing protein intrinsic disorder. Chem Rev 2014, 114:6561-6588.
    • (2014) Chem Rev , vol.114 , pp. 6561-6588
    • Habchi, J.1    Tompa, P.2    Longhi, S.3    Uversky, V.N.4
  • 11
    • 84925114160 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in cellular signalling and regulation
    • Wright P.E., Dyson H.J. Intrinsically disordered proteins in cellular signalling and regulation. Nat Rev Mol Cell Biol 2015, 16:18-29.
    • (2015) Nat Rev Mol Cell Biol , vol.16 , pp. 18-29
    • Wright, P.E.1    Dyson, H.J.2
  • 12
    • 79958037883 scopus 로고    scopus 로고
    • Constructing ensembles for intrinsically disordered proteins
    • Fisher C.K., Stultz C.M. Constructing ensembles for intrinsically disordered proteins. Curr Opin Struct Biol 2011, 21:426-431.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 426-431
    • Fisher, C.K.1    Stultz, C.M.2
  • 13
    • 47349126421 scopus 로고    scopus 로고
    • Mechanism of induced folding: both folding before binding and binding before folding can be realized in staphylococcal nuclease mutants
    • Onitsuka M., Kamikubo H., Yamazaki Y., Kataoka M. Mechanism of induced folding: both folding before binding and binding before folding can be realized in staphylococcal nuclease mutants. Proteins 2008, 72:837-847.
    • (2008) Proteins , vol.72 , pp. 837-847
    • Onitsuka, M.1    Kamikubo, H.2    Yamazaki, Y.3    Kataoka, M.4
  • 14
    • 79952741171 scopus 로고    scopus 로고
    • Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction
    • Bachmann A., Wildemann D., Praetorius F., Fischer G., Kiefhaber T. Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction. Proc Natl Acad Sci U S A 2011, 108:3952-3957.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3952-3957
    • Bachmann, A.1    Wildemann, D.2    Praetorius, F.3    Fischer, G.4    Kiefhaber, T.5
  • 16
    • 84873194008 scopus 로고    scopus 로고
    • Protein flexibility, not disorder, is intrinsic to molecular recognition
    • Janin J., Sternberg M.J.E. Protein flexibility, not disorder, is intrinsic to molecular recognition. F1000 Biol Rep 2013, 5.
    • (2013) F1000 Biol Rep , vol.5
    • Janin, J.1    Sternberg, M.J.E.2
  • 17
    • 84873198878 scopus 로고    scopus 로고
    • The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure
    • Uversky V.N., Dunker A.K. The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure. F1000 Biol Rep 2013, 5.
    • (2013) F1000 Biol Rep , pp. 5
    • Uversky, V.N.1    Dunker, A.K.2
  • 18
    • 0039789834 scopus 로고
    • Elementary steps in enzyme reactions (as studied by relaxation spectrometry)
    • Eigen M., Hammes G.G. Elementary steps in enzyme reactions (as studied by relaxation spectrometry). Adv Enzymol Relat Areas Mol Biol 1963, 25:1-38.
    • (1963) Adv Enzymol Relat Areas Mol Biol , vol.25 , pp. 1-38
    • Eigen, M.1    Hammes, G.G.2
  • 19
    • 67649589198 scopus 로고    scopus 로고
    • Reaching the protein folding speed limit with large, sub-microsecond pressure jumps
    • Dumont C., Emilsson T., Gruebele M. Reaching the protein folding speed limit with large, sub-microsecond pressure jumps. Nat Methods 2009, 6:515-519.
    • (2009) Nat Methods , vol.6 , pp. 515-519
    • Dumont, C.1    Emilsson, T.2    Gruebele, M.3
  • 20
    • 0031969090 scopus 로고    scopus 로고
    • A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale
    • Shastry M.C., Luck S.D., Roder H. A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale. Biophys J 1998, 74:2714-2721.
    • (1998) Biophys J , vol.74 , pp. 2714-2721
    • Shastry, M.C.1    Luck, S.D.2    Roder, H.3
  • 21
    • 77953263435 scopus 로고    scopus 로고
    • The role of mass transport limitation and surface heterogeneity in the biophysical characterization of macromolecular binding processes by SPR biosensing
    • Humana Press, N.J. Mol, M.J.E. Fischer (Eds.)
    • Schuck P., Zhao H. The role of mass transport limitation and surface heterogeneity in the biophysical characterization of macromolecular binding processes by SPR biosensing. Surface Plasmon Resonance 2010, 15-54. Humana Press. N.J. Mol, M.J.E. Fischer (Eds.).
    • (2010) Surface Plasmon Resonance , pp. 15-54
    • Schuck, P.1    Zhao, H.2
  • 22
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase K., Dyson H.J., Wright P.E. Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 2007, 447:1021-1025.
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 23
    • 84896336036 scopus 로고    scopus 로고
    • The binding mechanisms of intrinsically disordered proteins
    • Dogan J., Gianni S., Jemth P. The binding mechanisms of intrinsically disordered proteins. Phys Chem Chem Phys 2013, 10.1039/c3cp54226b.
    • (2013) Phys Chem Chem Phys
    • Dogan, J.1    Gianni, S.2    Jemth, P.3
  • 25
    • 84867280715 scopus 로고    scopus 로고
    • Fast association and slow transitions in the interaction between two intrinsically disordered protein domains
    • Dogan J., Schmidt T., Mu X., Engström Å, Jemth P. Fast association and slow transitions in the interaction between two intrinsically disordered protein domains. J Biol Chem 2012, 287:34316-34324.
    • (2012) J Biol Chem , vol.287 , pp. 34316-34324
    • Dogan, J.1    Schmidt, T.2    Mu, X.3    Engström, Å4    Jemth, P.5
  • 26
    • 84883780574 scopus 로고    scopus 로고
    • The transition state structure for coupled binding and folding of disordered protein domains
    • Dogan J., Mu X., Engström Å., Jemth P. The transition state structure for coupled binding and folding of disordered protein domains. Sci Rep 2013, 3:2076.
    • (2013) Sci Rep , vol.3 , pp. 2076
    • Dogan, J.1    Mu, X.2    Engström, Å.3    Jemth, P.4
  • 27
    • 84869218677 scopus 로고    scopus 로고
    • A folding-after-binding mechanism describes the recognition between the transactivation domain of c-Myb and the KIX domain of the CREB-binding protein
    • Gianni S., Morrone A., Giri R., Brunori M. A folding-after-binding mechanism describes the recognition between the transactivation domain of c-Myb and the KIX domain of the CREB-binding protein. Biochem Biophys Res Commun 2012, 428:205-209.
    • (2012) Biochem Biophys Res Commun , vol.428 , pp. 205-209
    • Gianni, S.1    Morrone, A.2    Giri, R.3    Brunori, M.4
  • 28
    • 84883780190 scopus 로고    scopus 로고
    • Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system
    • Giri R., Morrone A., Toto A., Brunori M., Gianni S. 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 U S A 2013, 110:14942-14947.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 14942-14947
    • Giri, R.1    Morrone, A.2    Toto, A.3    Brunori, M.4    Gianni, S.5
  • 29
    • 84886648634 scopus 로고    scopus 로고
    • Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX
    • Shammas S.L., Travis A.J., Clarke J. Remarkably fast coupled folding and binding of the intrinsically disordered transactivation domain of cMyb to CBP KIX. J Phys Chem B 2013, 117:13346-13356.
    • (2013) J Phys Chem B , vol.117 , pp. 13346-13356
    • Shammas, S.L.1    Travis, A.J.2    Clarke, J.3
  • 30
    • 84873828976 scopus 로고    scopus 로고
    • Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'
    • Rogers J.M., Steward A., Clarke J. Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'. J Am Chem Soc 2013, 135:1415-1422.
    • (2013) J Am Chem Soc , vol.135 , pp. 1415-1422
    • Rogers, J.M.1    Steward, A.2    Clarke, J.3
  • 31
    • 84897970680 scopus 로고    scopus 로고
    • Coupled folding and binding of the disordered protein PUMA does not require particular residual structure
    • Rogers J.M., Wong C.T., Clarke J. Coupled folding and binding of the disordered protein PUMA does not require particular residual structure. J Am Chem Soc 2014, 136:5197-5200.
    • (2014) J Am Chem Soc , vol.136 , pp. 5197-5200
    • Rogers, J.M.1    Wong, C.T.2    Clarke, J.3
  • 33
    • 80052021703 scopus 로고    scopus 로고
    • Kinetic recognition of the retinoblastoma tumor suppressor by a specific protein target
    • Chemes L.B., Sánchez I.E., de Prat-Gay G. Kinetic recognition of the retinoblastoma tumor suppressor by a specific protein target. J Mol Biol 2011, 412:267-284.
    • (2011) J Mol Biol , vol.412 , pp. 267-284
    • Chemes, L.B.1    Sánchez, I.E.2    de Prat-Gay, G.3
  • 35
    • 0019821957 scopus 로고
    • Binding of high affinity heparin to antithrombin. III. Stopped flow kinetic studies of the binding interaction
    • Olson S.T., Srinivasan K.R., Björk I., Shore J.D. Binding of high affinity heparin to antithrombin. III. Stopped flow kinetic studies of the binding interaction. J Biol Chem 1981, 256:11073-11079.
    • (1981) J Biol Chem , vol.256 , pp. 11073-11079
    • Olson, S.T.1    Srinivasan, K.R.2    Björk, I.3    Shore, J.D.4
  • 36
    • 84898953700 scopus 로고    scopus 로고
    • Distinguishing induced fit from conformational selection
    • Gianni S., Dogan J., Jemth P. Distinguishing induced fit from conformational selection. Biophys Chem 2014, 189C:33-39.
    • (2014) Biophys Chem , vol.189C , pp. 33-39
    • Gianni, S.1    Dogan, J.2    Jemth, P.3
  • 37
    • 84924362914 scopus 로고    scopus 로고
    • Fast helix formation in the B domain of protein A revealed by site-specific infrared probes
    • Davis C.M., Cooper A.K., Dyer R.B. Fast helix formation in the B domain of protein A revealed by site-specific infrared probes. Biochemistry 2015, 54:1758-1766.
    • (2015) Biochemistry , vol.54 , pp. 1758-1766
    • Davis, C.M.1    Cooper, A.K.2    Dyer, R.B.3
  • 38
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter M., Simon I., Friedrich P., Tompa P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J Mol Biol 2004, 338:1015-1026.
    • (2004) J Mol Biol , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 39
    • 84893454221 scopus 로고    scopus 로고
    • Helical propensity in an intrinsically disordered protein accelerates ligand binding
    • Iešmantavičius V., Dogan J., Jemth P., Teilum K., Kjaergaard M. Helical propensity in an intrinsically disordered protein accelerates ligand binding. Angew Chem Int Ed 2014, 53:1548-1551.
    • (2014) Angew Chem Int Ed , vol.53 , pp. 1548-1551
    • Iešmantavičius, V.1    Dogan, J.2    Jemth, P.3    Teilum, K.4    Kjaergaard, M.5
  • 41
    • 84908257600 scopus 로고    scopus 로고
    • Only kinetics can prove conformational selection
    • Dogan J., Jemth P. Only kinetics can prove conformational selection. Biophys J 2014, 107:1997-1998.
    • (2014) Biophys J , vol.107 , pp. 1997-1998
    • Dogan, J.1    Jemth, P.2
  • 42
    • 84923163065 scopus 로고    scopus 로고
    • Quantitative biophysical characterization of intrinsically disordered proteins
    • Gibbs E.B., Showalter S.A. Quantitative biophysical characterization of intrinsically disordered proteins. Biochemistry 2015, 54:1314-1326.
    • (2015) Biochemistry , vol.54 , pp. 1314-1326
    • Gibbs, E.B.1    Showalter, S.A.2
  • 43
    • 84921835922 scopus 로고    scopus 로고
    • Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR
    • Schneider R., Maurin D., Communie G., Kragelj J., Hansen D.F., Ruigrok R.W.H., Jensen M.R., Blackledge M. Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR. J Am Chem Soc 2015, 137:1220-1229.
    • (2015) J Am Chem Soc , vol.137 , pp. 1220-1229
    • Schneider, R.1    Maurin, D.2    Communie, G.3    Kragelj, J.4    Hansen, D.F.5    Ruigrok, R.W.H.6    Jensen, M.R.7    Blackledge, M.8
  • 44
    • 84938723752 scopus 로고    scopus 로고
    • Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding
    • Arai M., Sugase K., Dyson H.J., Wright P.E. Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding. Proc Natl Acad Sci U S A 2015, 112:9614-9619.
    • (2015) Proc Natl Acad Sci U S A , vol.112 , pp. 9614-9619
    • Arai, M.1    Sugase, K.2    Dyson, H.J.3    Wright, P.E.4
  • 46
    • 84863979552 scopus 로고    scopus 로고
    • Rate constants and mechanisms of intrinsically disordered proteins binding to structured targets
    • Zhou H.-X., Pang X., Lu C. Rate constants and mechanisms of intrinsically disordered proteins binding to structured targets. Phys Chem Chem Phys 2012, 14:10466-10476.
    • (2012) Phys Chem Chem Phys , vol.14 , pp. 10466-10476
    • Zhou, H.-X.1    Pang, X.2    Lu, C.3
  • 47
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions
    • Tompa P., Fuxreiter M. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 2008, 33:2-8.
    • (2008) Trends Biochem Sci , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 48
    • 84896886700 scopus 로고    scopus 로고
    • A frustrated binding interface for intrinsically disordered proteins
    • Jemth P., Mu X., EngströmF Å., Dogan J. A frustrated binding interface for intrinsically disordered proteins. J Biol Chem 2014, 289:5528-5533.
    • (2014) J Biol Chem , vol.289 , pp. 5528-5533
    • Jemth, P.1    Mu, X.2    EngströmF, Å.3    Dogan, J.4
  • 49
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: a synthesis
    • Bryngelson J.D., Onuchic J.N., Socci N.D., Wolynes P.G. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 1995, 21:167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 50
    • 84856708599 scopus 로고    scopus 로고
    • Intrinsic disorder: signaling via highly specific but short-lived association
    • Zhou H.-X. Intrinsic disorder: signaling via highly specific but short-lived association. Trends Biochem Sci 2012, 37:43-48.
    • (2012) Trends Biochem Sci , vol.37 , pp. 43-48
    • Zhou, H.-X.1
  • 51
    • 84938629771 scopus 로고    scopus 로고
    • Binding rate constants reveal distinct features of disordered protein domains
    • Dogan J., Jonasson J., Andersson E., Jemth P. Binding rate constants reveal distinct features of disordered protein domains. Biochemistry 2015, 54:4741-4750.
    • (2015) Biochemistry , vol.54 , pp. 4741-4750
    • Dogan, J.1    Jonasson, J.2    Andersson, E.3    Jemth, P.4
  • 52
    • 34249863018 scopus 로고    scopus 로고
    • Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53
    • Teufel D.P., Freund S.M., Bycroft M., Fersht A.R. Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. Proc. Natl Acad Sci U S A 2007, 104:7009-7014.
    • (2007) Proc. Natl Acad Sci U S A , vol.104 , pp. 7009-7014
    • Teufel, D.P.1    Freund, S.M.2    Bycroft, M.3    Fersht, A.R.4
  • 55
    • 84857653889 scopus 로고    scopus 로고
    • The transition state of coupled folding and binding for a flexible β-finger
    • Karlsson O.A., Chi C.N., Engström A., Jemth P. The transition state of coupled folding and binding for a flexible β-finger. J Mol Biol 2012, 417:253-261.
    • (2012) J Mol Biol , vol.417 , pp. 253-261
    • Karlsson, O.A.1    Chi, C.N.2    Engström, A.3    Jemth, P.4
  • 56
    • 84890859432 scopus 로고    scopus 로고
    • Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners
    • Hill S.A., Kwa L.G., Shammas S.L., Lee J.C., Clarke J. Mechanism of assembly of the non-covalent spectrin tetramerization domain from intrinsically disordered partners. J Mol Biol 2014, 426:21-35.
    • (2014) J Mol Biol , vol.426 , pp. 21-35
    • Hill, S.A.1    Kwa, L.G.2    Shammas, S.L.3    Lee, J.C.4    Clarke, J.5
  • 57
    • 26944450513 scopus 로고    scopus 로고
    • An electrostatic steering mechanism of Cdc42 recognition by Wiskott-Aldrich syndrome proteins
    • Hemsath L., Dvorsky R., Fiegen D., Carlier M.-F., Ahmadian M.R. An electrostatic steering mechanism of Cdc42 recognition by Wiskott-Aldrich syndrome proteins. Mol Cell 2005, 20:313-324.
    • (2005) Mol Cell , vol.20 , pp. 313-324
    • Hemsath, L.1    Dvorsky, R.2    Fiegen, D.3    Carlier, M.-F.4    Ahmadian, M.R.5
  • 58
    • 84865689638 scopus 로고    scopus 로고
    • Electrostatically accelerated coupled binding and folding of intrinsically disordered proteins
    • Ganguly D., Otieno S., Waddell B., Iconaru L., Kriwacki R.W., Chen J. Electrostatically accelerated coupled binding and folding of intrinsically disordered proteins. J Mol Biol 2012, 422:674-684.
    • (2012) J Mol Biol , vol.422 , pp. 674-684
    • Ganguly, D.1    Otieno, S.2    Waddell, B.3    Iconaru, L.4    Kriwacki, R.W.5    Chen, J.6
  • 59
    • 65249099497 scopus 로고    scopus 로고
    • Fundamental aspects of protein-protein association kinetics
    • Schreiber G., Haran G., Zhou H.-X. Fundamental aspects of protein-protein association kinetics. Chem Rev 2009, 109:839-860.
    • (2009) Chem Rev , vol.109 , pp. 839-860
    • Schreiber, G.1    Haran, G.2    Zhou, H.-X.3
  • 60
    • 84906328511 scopus 로고    scopus 로고
    • Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants
    • Shammas S.L., Travis A.J., Clarke J. Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants. Proc Natl Acad Sci U S A 2014, 111:12055-12060.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 12055-12060
    • Shammas, S.L.1    Travis, A.J.2    Clarke, J.3
  • 61
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: the fly-casting mechanism
    • Shoemaker B.A., Portman J.J., Wolynes P.G. Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc Natl Acad Sci U S A 2000, 97:8868-8873.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 62
    • 84888242647 scopus 로고    scopus 로고
    • Electrostatically accelerated encounter and folding for facile recognition of intrinsically disordered proteins
    • Ganguly D., Zhang W., Chen J. Electrostatically accelerated encounter and folding for facile recognition of intrinsically disordered proteins. PLoS Comput Biol 2013, 9:e1003363.
    • (2013) PLoS Comput Biol , vol.9 , pp. e1003363
    • Ganguly, D.1    Zhang, W.2    Chen, J.3
  • 63
    • 84885065793 scopus 로고    scopus 로고
    • Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein
    • Wang Y., Chu X., Longhi S., Roche P., Han W., Wang E., Wang J. Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein. Proc Natl Acad Sci U S A 2013, 110:E3743-E3752.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E3743-E3752
    • Wang, Y.1    Chu, X.2    Longhi, S.3    Roche, P.4    Han, W.5    Wang, E.6    Wang, J.7
  • 64
    • 84900021556 scopus 로고    scopus 로고
    • Discriminating binding mechanisms of an intrinsically disordered protein via a multi-state coarse-grained model
    • Knott M., Best R.B. Discriminating binding mechanisms of an intrinsically disordered protein via a multi-state coarse-grained model. J Chem Phys 2014, 140:175102.
    • (2014) J Chem Phys , vol.140 , pp. 175102
    • Knott, M.1    Best, R.B.2
  • 67
    • 0346733326 scopus 로고    scopus 로고
    • Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB-binding protein
    • Demarest S.J., Deechongkit S., Dyson H.J., Evans R.M., Wright P.E. Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB-binding protein. Protein Sci 2004, 13:203-210.
    • (2004) Protein Sci , vol.13 , pp. 203-210
    • Demarest, S.J.1    Deechongkit, S.2    Dyson, H.J.3    Evans, R.M.4    Wright, P.E.5
  • 68
    • 77955442470 scopus 로고    scopus 로고
    • Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP
    • Kjaergaard M., Teilum K., Poulsen F.M. Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. Proc Natl Acad Sci U S A 2010, 107:12535-12540.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 12535-12540
    • Kjaergaard, M.1    Teilum, K.2    Poulsen, F.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.