메뉴 건너뛰기




Volumn 117, Issue 12, 2013, Pages 3298-3307

Molecular dynamics simulations of yeast F1-atpase before and after 16 rotation of the γ subunit

Author keywords

[No Author keywords available]

Indexed keywords

MOLECULAR DYNAMICS; YEAST;

EID: 84875702025     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp312499u     Document Type: Article
Times cited : (18)

References (57)
  • 1
    • 0020570950 scopus 로고
    • 1): Biochemical and Molecular Biological Approaches
    • 1): Biochemical and Molecular Biological Approaches Microbiol. Rev. 1983, 47, 285-312
    • (1983) Microbiol. Rev. , vol.47 , pp. 285-312
    • Futai, M.1    Kanazawa, H.2
  • 2
    • 0024354291 scopus 로고
    • +-ATPase): Results by Combined Biochemical and Molecular Biological Approaches
    • +-ATPase): Results by Combined Biochemical and Molecular Biological Approaches Annu. Rev. Biochem. 1989, 58, 111-136
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 111-136
    • Futai, M.1    Noumi, T.2    Maeda, M.3
  • 3
    • 0025338413 scopus 로고
    • The Proton-Translocating ATPase of Escherichia coli
    • Senior, A. E. The Proton-Translocating ATPase of Escherichia coli Annu. Rev. Biophys. Biophys. Chem. 1990, 19, 7-41
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 7-41
    • Senior, A.E.1
  • 4
    • 0027232750 scopus 로고
    • ATP Synthases. Structure, Reaction Center, Mechanism, and Regulation of One of Nature's Most Unique Machines
    • Pedersen, P. L.; Amzel, L. M. ATP Synthases. Structure, Reaction Center, Mechanism, and Regulation of One of Nature's Most Unique Machines J. Biol. Chem. 1993, 268, 9937-9940
    • (1993) J. Biol. Chem. , vol.268 , pp. 9937-9940
    • Pedersen, P.L.1    Amzel, L.M.2
  • 5
    • 0031008228 scopus 로고    scopus 로고
    • The ATP Synthase -A Splendid Molecular Machine
    • Boyer, P. D. The ATP Synthase-A Splendid Molecular Machine Annu. Rev. Biochem. 1997, 66, 717-749
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 6
    • 0032544312 scopus 로고    scopus 로고
    • ATP Synthesis by Rotary Catalysis (Nobel Lecture)
    • Walker, J. E. ATP Synthesis by Rotary Catalysis (Nobel Lecture) Angew. Chem., Int. Ed. 1998, 37, 2308-2319
    • (1998) Angew. Chem., Int. Ed. , vol.37 , pp. 2308-2319
    • Walker, J.E.1
  • 7
    • 0034737965 scopus 로고    scopus 로고
    • ATP Synthase: What We Know about ATP Hydrolysis and What We Do Not Know about ATP Synthesis
    • Weber, J.; Senior, A. E. ATP Synthase: What We Know About ATP Hydrolysis and What We Do Not Know About ATP Synthesis Biochim. Biophys. Acta 2000, 1458, 300-309
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 300-309
    • Weber, J.1    Senior, A.E.2
  • 13
    • 0033581879 scopus 로고    scopus 로고
    • Structural Changes Linked to Proton Translocation by Subunit c of the ATP Synthase
    • Rastogi, V. K.; Girvin, M. E. Structural Changes Linked to Proton Translocation by Subunit c of the ATP Synthase Nature 1999, 402, 263-268
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 15
    • 0032568695 scopus 로고    scopus 로고
    • 1-ATPase is a Highly Efficient Motor That Rotates with Discrete 120-degree Steps
    • 1-ATPase is a Highly Efficient Motor That Rotates with Discrete 120-degree Steps Cell 1998, 93, 1117-1124
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita Jr., K.3    Yoshida, M.4
  • 33
    • 77954245699 scopus 로고    scopus 로고
    • 1-ATPase: A Molecular Dynamics Study
    • 1-ATPase: A Molecular Dynamics Study J. Comput. Chem. 2010, 31, 2175-2185
    • (2010) J. Comput. Chem. , vol.31 , pp. 2175-2185
    • Ito, Y.1    Ikeguchi, M.2
  • 34
    • 79952607783 scopus 로고    scopus 로고
    • 1-ATPase β Subunit Revealed by Free Energy Simulations
    • 1-ATPase β Subunit Revealed by Free Energy Simulations J. Am. Chem. Soc. 2011, 133, 3372-3380
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 3372-3380
    • Ito, Y.1    Oroguchi, T.2    Ikeguchi, M.3
  • 38
    • 79961236945 scopus 로고    scopus 로고
    • High-Speed Atomic Force Microscopy Reveals Rotary Catalysis of Rotorless
    • Uchihashi, T.; Iino, R.; Ando, T.; Noji, H. High-Speed Atomic Force Microscopy Reveals Rotary Catalysis of Rotorless Science 2011, 333, 755-758
    • (2011) Science , vol.333 , pp. 755-758
    • Uchihashi, T.1    Iino, R.2    Ando, T.3    Noji, H.4
  • 41
    • 18144418170 scopus 로고    scopus 로고
    • Protein Structural Change upon Ligand Binding: Linear Response Theory
    • Ikeguchi, M.; Ueno, J.; Sato, M.; Kidera, A. Protein Structural Change upon Ligand Binding: Linear Response Theory Phys. Rev. Lett. 2005, 94, 078102
    • (2005) Phys. Rev. Lett. , vol.94 , pp. 078102
    • Ikeguchi, M.1    Ueno, J.2    Sato, M.3    Kidera, A.4
  • 43
    • 0027136282 scopus 로고
    • Comparative Protein Modelling by Satisfaction of Spatial Restraints
    • Sali, A.; Blundell, T. L. Comparative Protein Modelling by Satisfaction of Spatial Restraints J. Mol. Biol. 1993, 234, 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 45
    • 3042581007 scopus 로고    scopus 로고
    • Flexible Structure Alignment by Chaining Aligned Fragment Pairs Allowing Twists
    • Ye, Y.; Godzik, A. Flexible Structure Alignment by Chaining Aligned Fragment Pairs Allowing Twists Bioinformatics 2003, 19 (Suppl 2) II246-II255
    • (2003) Bioinformatics , vol.19 , Issue.SUPPL. 2
    • Ye, Y.1    Godzik, A.2
  • 46
    • 1442281404 scopus 로고    scopus 로고
    • Partial Rigid-Body Dynamics in NPT, NPAT and NPγT Ensembles for Proteins and Membranes
    • Ikeguchi, M. Partial Rigid-Body Dynamics in NPT, NPAT and NPγT Ensembles for Proteins and Membranes J. Comput. Chem. 2004, 25, 529-541
    • (2004) J. Comput. Chem. , vol.25 , pp. 529-541
    • Ikeguchi, M.1
  • 47
    • 0041784950 scopus 로고    scopus 로고
    • All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins
    • MacKerell, A. D. All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins J. Phys. Chem. B 1998, 102, 3586-3616
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1
  • 48
    • 3142714765 scopus 로고    scopus 로고
    • Extending the Treatment of Backbone Energetics in Protein Force Fields: Limitations of Gas-Phase Quantum Mechanics in Reproducing Protein Conformational Distributions in Molecular Dynamics Simulations
    • MacKerell, A. D., Jr.; Feig, M.; Brooks, C. L., III. Extending the Treatment of Backbone Energetics in Protein Force Fields: Limitations of Gas-Phase Quantum Mechanics in Reproducing Protein Conformational Distributions in Molecular Dynamics Simulations J. Comput. Chem. 2004, 25, 1400-1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 51
    • 67649373298 scopus 로고    scopus 로고
    • Intrinsic Dynamics of Restriction Endonuclease EcoO109I Studied by Molecular Dynamics Simulations and X-Ray Scattering Data Analysis
    • Oroguchi, T.; Hashimoto, H.; Shimizu, T.; Sato, M.; Ikeguchi, M. Intrinsic Dynamics of Restriction Endonuclease EcoO109I Studied by Molecular Dynamics Simulations and X-Ray Scattering Data Analysis Biophys. J. 2009, 96, 2808-2822
    • (2009) Biophys. J. , vol.96 , pp. 2808-2822
    • Oroguchi, T.1    Hashimoto, H.2    Shimizu, T.3    Sato, M.4    Ikeguchi, M.5
  • 52
    • 84864265187 scopus 로고    scopus 로고
    • 1-ATPase before and after 16-degree Rotation of the γ Subunit: Theoretical Analysis Focused on the Water-Entropy Effect
    • 1-ATPase before and after 16-degree Rotation of the γ Subunit: Theoretical Analysis Focused on the Water-Entropy Effect J. Chem. Phys. 2012, 137, 035102
    • (2012) J. Chem. Phys. , vol.137 , pp. 035102
    • Yoshidome, T.1    Ito, Y.2    Matubayasi, N.3    Ikeguchi, M.4    Kinoshita, M.5
  • 53
    • 0030575490 scopus 로고    scopus 로고
    • Interaction between Macroparticles in Aqueous Electrolytes
    • Kinoshita, M.; Iba, S.; Harada, M. Interaction between Macroparticles in Aqueous Electrolytes J. Chem. Phys. 1996, 105, 2487-2499
    • (1996) J. Chem. Phys. , vol.105 , pp. 2487-2499
    • Kinoshita, M.1    Iba, S.2    Harada, M.3
  • 54
    • 23844468461 scopus 로고    scopus 로고
    • Potential of Mean Force between Solute Atoms in Salt Solution: Effects Due to Salt Species and Relevance to Conformational Transition of Biomolecules
    • Kinoshita, M.; Harano, Y. Potential of Mean Force between Solute Atoms in Salt Solution: Effects Due to Salt Species and Relevance to Conformational Transition of Biomolecules Bull. Chem. Soc. Jpn. 2005, 78, 1431-1441
    • (2005) Bull. Chem. Soc. Jpn. , vol.78 , pp. 1431-1441
    • Kinoshita, M.1    Harano, Y.2
  • 55
    • 79953855777 scopus 로고    scopus 로고
    • 1-ATPase: Interplay among Enzyme Structures, Catalysis, and Rotations
    • 1-ATPase: Interplay among Enzyme Structures, Catalysis, and Rotations Structure 2011, 19, 588-598
    • (2011) Structure , vol.19 , pp. 588-598
    • Okazaki, K.1    Takada, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.