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Volumn 18, Issue 5, 2007, Pages 1619-1624

Design of a thermocontrollable protein complex

Author keywords

[No Author keywords available]

Indexed keywords

ELASTIN; ENERGY TRANSFER; GLYCOPROTEINS;

EID: 34648837116     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc070120x     Document Type: Article
Times cited : (8)

References (22)
  • 2
    • 0038635001 scopus 로고    scopus 로고
    • Light-driven open-close motion of chiral molecular scissors
    • Muraoka, T., Kinbara, K., Kobayashi, Y., and Aida, T. (2003) Light-driven open-close motion of chiral molecular scissors. J. Am. Chem. Soc. 125, 5612-5613.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 5612-5613
    • Muraoka, T.1    Kinbara, K.2    Kobayashi, Y.3    Aida, T.4
  • 3
    • 4043131865 scopus 로고    scopus 로고
    • Light-driven molecular hinge: A new molecular machine showing a light-intensity-dependent photoresponse that utilizes the trans-cis isomerization of azobenzene
    • Norikane, Y., and Tamaoki, N. (2004) Light-driven molecular hinge: a new molecular machine showing a light-intensity-dependent photoresponse that utilizes the trans-cis isomerization of azobenzene. Org. Lett. 6 (15), 2595-2598.
    • (2004) Org. Lett , vol.6 , Issue.15 , pp. 2595-2598
    • Norikane, Y.1    Tamaoki, N.2
  • 4
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji, H., Yasuda, R., Yoshida, M., and Kinosita, K. (1997) Direct observation of the rotation of F1-ATPase. Nature (London) 386, 299-302.
    • (1997) Nature (London) , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita, K.4
  • 5
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometer steps
    • Finer, J. T., Simmons, R. M., and Spudich, J. A. (1994) Single myosin molecule mechanics: piconewton forces and nanometer steps. Nature (London) 368, 113-119.
    • (1994) Nature (London) , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 6
    • 1442326719 scopus 로고    scopus 로고
    • Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and single-particle image analysis
    • Suzuki, H., Yonekura, K., and Namba, K. (2004) Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and single-particle image analysis. J. Mol. Biol. 337, 105-113.
    • (2004) J. Mol. Biol , vol.337 , pp. 105-113
    • Suzuki, H.1    Yonekura, K.2    Namba, K.3
  • 8
    • 0033539646 scopus 로고    scopus 로고
    • An engineered minidomain containing an elastin turn exhibits a reversible temperature-induced IgG binding
    • Reiersen, H., and Rees, A. R. (1999) An engineered minidomain containing an elastin turn exhibits a reversible temperature-induced IgG binding. Biochemistry 38, 14897-14905.
    • (1999) Biochemistry , vol.38 , pp. 14897-14905
    • Reiersen, H.1    Rees, A.R.2
  • 9
    • 0141534348 scopus 로고    scopus 로고
    • DNA-templated self-assembly of protein arrays and highly conductive nanowires
    • Yan, H., Park, S. H., Finkelstein, G., Reif, J. H., and LaBean, T. H. (2003) DNA-templated self-assembly of protein arrays and highly conductive nanowires. Science 301, 1882-1884.
    • (2003) Science , vol.301 , pp. 1882-1884
    • Yan, H.1    Park, S.H.2    Finkelstein, G.3    Reif, J.H.4    LaBean, T.H.5
  • 10
    • 24644501619 scopus 로고    scopus 로고
    • Charged polypeptide vesicles with controllable diameter
    • Holowka, E. P., Pochan, D. J., and Deming, T. J. (2005) Charged polypeptide vesicles with controllable diameter. J. Am. Chem. Soc. 127, 12423-12428.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 12423-12428
    • Holowka, E.P.1    Pochan, D.J.2    Deming, T.J.3
  • 13
    • 0032922665 scopus 로고    scopus 로고
    • Crystal structure of a designed, thermostable, heterotrimeric coiled coil
    • Nautiyal, S., and Alber, T. (1999) Crystal structure of a designed, thermostable, heterotrimeric coiled coil. Protein Sci. 8, 84-90.
    • (1999) Protein Sci , vol.8 , pp. 84-90
    • Nautiyal, S.1    Alber, T.2
  • 14
    • 0027590739 scopus 로고
    • Self-assembly of bioelastomeric stmctures from solutions: Meanfield critical behavior and Flory-Huggins free energy of interactions
    • Sciortino, F., Prasad, K. U., Urry, D. W., and Palma, M. U. (1993) Self-assembly of bioelastomeric stmctures from solutions: meanfield critical behavior and Flory-Huggins free energy of interactions. Biopolymers 33, 743-752.
    • (1993) Biopolymers , vol.33 , pp. 743-752
    • Sciortino, F.1    Prasad, K.U.2    Urry, D.W.3    Palma, M.U.4
  • 15
    • 0038245213 scopus 로고    scopus 로고
    • Mechanics of elastin: Molecular mechanism of biological elasticity and its relationship to contraction
    • Urry, D. W., and Parker, T. M. (2002) Mechanics of elastin: molecular mechanism of biological elasticity and its relationship to contraction. J. Muscle Res. Cell Motil. 23, 543-559.
    • (2002) J. Muscle Res. Cell Motil , vol.23 , pp. 543-559
    • Urry, D.W.1    Parker, T.M.2
  • 17
    • 0038388786 scopus 로고    scopus 로고
    • Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers
    • Urry, D. W. (1997) Physical chemistry of biological free energy transduction as demonstrated by elastic protein-based polymers. J. Phys. Chem. B 101, 11007-11028.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 11007-11028
    • Urry, D.W.1
  • 18
    • 0036200174 scopus 로고    scopus 로고
    • Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: Examples from the elastin-like polypeptide system
    • Meyer, D. E., and Chilkoti, A. (2002) Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: examples from the elastin-like polypeptide system. Biomacromolecules 3, 357-367.
    • (2002) Biomacromolecules , vol.3 , pp. 357-367
    • Meyer, D.E.1    Chilkoti, A.2
  • 19
    • 0034878076 scopus 로고    scopus 로고
    • Protein purification by fusion with an environmentally responsive elastin-like polypeptide: Effect of polypeptide length on the purification of thioredoxin
    • Meyer, D. E., Trabbic-Carlson, K., and Chilkoti, A. (2001) Protein purification by fusion with an environmentally responsive elastin-like polypeptide: effect of polypeptide length on the purification of thioredoxin. Biotechnol. Prog. 17, 720-728.
    • (2001) Biotechnol. Prog , vol.17 , pp. 720-728
    • Meyer, D.E.1    Trabbic-Carlson, K.2    Chilkoti, A.3
  • 20
    • 0032739304 scopus 로고    scopus 로고
    • Purification of recombinant proteins by fusion with thermally-responsive polypeptides
    • Meyer, D. E., and Chilkoti, A. (1999) Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat. Biotechnol. 17, 1112-1115.
    • (1999) Nat. Biotechnol , vol.17 , pp. 1112-1115
    • Meyer, D.E.1    Chilkoti, A.2
  • 22
    • 7444241366 scopus 로고    scopus 로고
    • De novo design of defined helical bundles in membrane environments
    • Bilgiçer, B., and Kumar, K. (2004) De novo design of defined helical bundles in membrane environments. Proc. Natl. Acad. Sci. U.S.A. 101, 15324-15329.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 15324-15329
    • Bilgiçer, B.1    Kumar, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.