메뉴 건너뛰기




Volumn 91, Issue 6, 2006, Pages 2055-2062

Coupling of global and local vibrational modes in dynamic allostery of proteins

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN DERIVATIVE;

EID: 33748442882     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.082180     Document Type: Article
Times cited : (55)

References (32)
  • 1
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • Gunasekaran, K., B. Ma, and R. Nussinov. 2004. Is allostery an intrinsic property of all dynamic proteins? Proteins. 57:433-443.
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.1    Ma, B.2    Nussinov, R.3
  • 2
    • 0021658956 scopus 로고
    • Allostery without conformational change - A plausible model
    • Cooper, A., and D. T. F. Dryden. 1984. Allostery without conformational change - a plausible model. Eur. Biophys. J. Biophys. Lett. 11:103-109.
    • (1984) Eur. Biophys. J. Biophys. Lett. , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.F.2
  • 3
    • 19544377327 scopus 로고    scopus 로고
    • Coarse-grained model of entropic allostery
    • Hawkins, R. J., and T. C. B. McLeish. 2004. Coarse-grained model of entropic allostery. Phys. Rev. Lett. 93:098104.
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 098104
    • Hawkins, R.J.1    McLeish, T.C.B.2
  • 4
    • 33747137334 scopus 로고    scopus 로고
    • Dynamic allostery of protein α-helical coiled-coils
    • Hawkins, R. J., and T. C. B. McLeish. 2006. Dynamic allostery of protein α-helical coiled-coils. J. Roy. Soc. Interf. 3:125-138.
    • (2006) J. Roy. Soc. Interf. , vol.3 , pp. 125-138
    • Hawkins, R.J.1    McLeish, T.C.B.2
  • 5
    • 0030433170 scopus 로고    scopus 로고
    • Protein dynamics and conformational transitions in allosteric proteins
    • Jardetzky, O. 1996. Protein dynamics and conformational transitions in allosteric proteins. Prog. Biophys. Mol. Biol. 65:171-219.
    • (1996) Prog. Biophys. Mol. Biol. , vol.65 , pp. 171-219
    • Jardetzky, O.1
  • 6
    • 0242585455 scopus 로고    scopus 로고
    • Configurational entropy and cooperativity between ligand binding and dimerization in glycopeptide antibiotics
    • Jusuf, S., P. J. Loll, and P. H. Axelsen. 2003. Configurational entropy and cooperativity between ligand binding and dimerization in glycopeptide antibiotics. J. Am. Chem. Soc. 125:3988-3994.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3988-3994
    • Jusuf, S.1    Loll, P.J.2    Axelsen, P.H.3
  • 7
    • 0032555216 scopus 로고    scopus 로고
    • The allosteric mechanism of the chaperonin GroEL: A dynamic analysis
    • Ma, J., and M. Karplus. 1998. The allosteric mechanism of the chaperonin GroEL: a dynamic analysis. Proc. Natl. Acad. Sci. USA. 95:8502-8507.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8502-8507
    • Ma, J.1    Karplus, M.2
  • 8
    • 18844409482 scopus 로고    scopus 로고
    • Quantifying allosteric effects in proteins
    • Ming, D., and M. E. Wall. 2005. Quantifying allosteric effects in proteins. Proteins. 59:697-707.
    • (2005) Proteins , vol.59 , pp. 697-707
    • Ming, D.1    Wall, M.E.2
  • 9
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar, I., A. Atilgan, and B. Erman. 1997. Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Fold. Des. 2:173-181.
    • (1997) Fold. Des. , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.2    Erman, B.3
  • 10
    • 0141792364 scopus 로고    scopus 로고
    • Allosteric changes in protein structure computed by a simple mechanical model: Hemoglobin T ↔ R2 transition
    • Xu, C., D. Tobi, and I. Bahar. 2003. Allosteric changes in protein structure computed by a simple mechanical model: hemoglobin T ↔ R2 transition. J. Mol. Biol. 333:153-168.
    • (2003) J. Mol. Biol. , vol.333 , pp. 153-168
    • Xu, C.1    Tobi, D.2    Bahar, I.3
  • 11
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama, F., and Y. H. Sanejouand. 2001. Conformational change of proteins arising from normal mode calculations. Protein Eng. 14:1-6.
    • (2001) Protein Eng. , vol.14 , pp. 1-6
    • Tama, F.1    Sanejouand, Y.H.2
  • 13
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from NMR spectroscopy
    • Wand, A. J. 2001. Dynamic activation of protein function: a view emerging from NMR spectroscopy. Nat. Struct. Biol. 8:926-931.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 15
    • 0346220393 scopus 로고    scopus 로고
    • The role of dynamics in allosteric regulation
    • Kern, D., and E. R. P. Zuiderweg. 2003. The role of dynamics in allosteric regulation. Curr. Opin. Struct. Biol. 13:748-757.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 748-757
    • Kern, D.1    Zuiderweg, E.R.P.2
  • 16
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • Volkman, B., D. Lipson, D. Wemmer, and D. Kern. 2001. Two-state allosteric behavior in a single-domain signaling protein. Science. 291:2429-2433.
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.1    Lipson, D.2    Wemmer, D.3    Kern, D.4
  • 18
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier, A., and L. E. Kay. 2006. New tools provide new insights in NMR studies of protein dynamics. Science. 312:224-228.
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 19
    • 29144461924 scopus 로고    scopus 로고
    • Coupled protein domain motion in TAQ polymerase revealed by neutron spin-echo spectroscopy
    • Bu, Z., R. Biehl, M. Monkenbusch, D. Richter, and D. J. E. Callaway. 2005. Coupled protein domain motion in TAQ polymerase revealed by neutron spin-echo spectroscopy. Proc. Natl. Acad. Sci. USA. 102:17646-17651.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17646-17651
    • Bu, Z.1    Biehl, R.2    Monkenbusch, M.3    Richter, D.4    Callaway, D.J.E.5
  • 20
    • 0034641670 scopus 로고    scopus 로고
    • Tryptophan fluorescence reveals the conformational state of a dynamic loop in recombinant porcine fructose-1,6-bisphosphatase
    • Nelson, S. W., C. V. Iancu, J.-Y. Choe, R. B. Honzatko, and H. J. Fromm. 2000. Tryptophan fluorescence reveals the conformational state of a dynamic loop in recombinant porcine fructose-1,6-bisphosphatase. Biochemistry. 39:11100-11106.
    • (2000) Biochemistry , vol.39 , pp. 11100-11106
    • Nelson, S.W.1    Iancu, C.V.2    Choe, J.-Y.3    Honzatko, R.B.4    Fromm, H.J.5
  • 21
    • 0036385839 scopus 로고    scopus 로고
    • Elastic properties of proteins: Insight on the folding process and evolutionary selection of native structures
    • Micheletti, C., G. Lattanzi, and A. Maritan. 2002. Elastic properties of proteins: insight on the folding process and evolutionary selection of native structures. J. Mol. Biol. 321:909-921.
    • (2002) J. Mol. Biol. , vol.321 , pp. 909-921
    • Micheletti, C.1    Lattanzi, G.2    Maritan, A.3
  • 22
    • 0028238102 scopus 로고
    • Calorimetric studies of the energetics of protein-DNA interactions in the Escherichia coli methionine repressor (MetJ) system
    • Cooper, A., A. McAlpine, and P. G. Stockley. 1994. Calorimetric studies of the energetics of protein-DNA interactions in the Escherichia coli methionine repressor (MetJ) system. FEBS Lett. 348:41-45.
    • (1994) FEBS Lett. , vol.348 , pp. 41-45
    • Cooper, A.1    McAlpine, A.2    Stockley, P.G.3
  • 25
    • 0026641755 scopus 로고
    • Crystal structure of the Met repressor-operator complexes at 2.8 Å resolution reveals DNA recognition by β-strands
    • Somers, W. S., and S. E. V. Phillips. 1992. Crystal structure of the Met repressor-operator complexes at 2.8 Å resolution reveals DNA recognition by β-strands. Nature. 387:359-393.
    • (1992) Nature , vol.387 , pp. 359-393
    • Somers, W.S.1    Phillips, S.E.V.2
  • 26
    • 0030605513 scopus 로고    scopus 로고
    • Structure and function of Escherichia coli Met repressor: Similarities and contrasts with Trp repressor
    • Phillips, S. E., and P. G. Stockley. 1996. Structure and function of Escherichia coli Met repressor: similarities and contrasts with Trp repressor. Philos. Trans. R. Soc. Lond. B Biol. Sci. 351:527-535.
    • (1996) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.351 , pp. 527-535
    • Phillips, S.E.1    Stockley, P.G.2
  • 27
    • 0024462909 scopus 로고
    • Three-dimensional crystal structures of Escherichia coli Met repressor with and without corepressor
    • Rafferty, J. B., W. S. Somers, I. Saint-Girons, and S. E. V. Phillips. 1989. Three-dimensional crystal structures of Escherichia coli Met repressor with and without corepressor. Nature. 341:705-710.
    • (1989) Nature , vol.341 , pp. 705-710
    • Rafferty, J.B.1    Somers, W.S.2    Saint-Girons, I.3    Phillips, S.E.V.4
  • 28
    • 0028773287 scopus 로고
    • Electrostatic activation of Escherichia coli methionine repressor
    • Phillips, K., and S. E. V. Phillips. 1994. Electrostatic activation of Escherichia coli methionine repressor. Structure. 2:309-316.
    • (1994) Structure , vol.2 , pp. 309-316
    • Phillips, K.1    Phillips, S.E.V.2
  • 29
    • 3242875210 scopus 로고    scopus 로고
    • ElNémo: A normal mode web server for protein movement analysis and the generation of templates for molecular replacement
    • Suhre, K., and S. Yves-Henri. 2004. ElNémo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Res. 32:W610-W614.
    • (2004) Nucleic Acids Res , vol.32
    • Suhre, K.1    Yves-Henri, S.2
  • 30
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude elastic motions in proteins from a single parameter, atomic analysis
    • Tirion, M. M. 1996. Large amplitude elastic motions in proteins from a single parameter, atomic analysis. Phys. Rev. Lett. 77:1905-1908.
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 1905-1908
    • Tirion, M.M.1
  • 31
    • 4644324871 scopus 로고    scopus 로고
    • Entropy/enthalpy compensation: Hydrophobic effect, micelles and protein complexes
    • Fisicaro, E., C. Compari, and A. Braibanti. 2004. Entropy/enthalpy compensation: hydrophobic effect, micelles and protein complexes. Phys. Chem. Chem. Phys. 6:4156-4166.
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4156-4166
    • Fisicaro, E.1    Compari, C.2    Braibanti, A.3
  • 32
    • 4344649812 scopus 로고    scopus 로고
    • CBF β allosterically regulates the RUNX1 runt domain via a dynamic conformational equilibrium
    • Yan, J., Y. Liu, S. M. Lukasik, N. A. Speck, and J. H. Bushweller. 2004. CBF β allosterically regulates the RUNX1 runt domain via a dynamic conformational equilibrium. Nat. Struct. Mol. Biol. 11:901-906.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 901-906
    • Yan, J.1    Liu, Y.2    Lukasik, S.M.3    Speck, N.A.4    Bushweller, J.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.