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Structural variation of molecular chaperone group Ⅱ by crystallography and cryo-electron microscopy

Structural variation of molecular chaperone group Ⅱ by crystallography and cryo-electron microscopy
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摘要 Chaperonins, a class of molecular chaperones, are oligomeric complexes acting as a protein-folding chamber in an ATP-dependent manner. Chaperonins have been classifed
出处 《生物物理学报》 CAS CSCD 北大核心 2009年第S1期7-8,共2页 Acta Biophysica Sinica
关键词 CHAPERONIN THERMOSOME cryo-electron MICROSCOPY SYMMETRY CONFORMATION change chaperonin, thermosome, cryo-electron microscopy, symmetry, conformation change
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参考文献3

  • 1Guy Schoehn,Elsie Q.R,Jose L. Jimenez,Andrzej Joachimiak,Helen R.Saibil.Three Conformations of an Archaeal Chaperonin, TF55 from Sulfolobus shibatae[].Journal of Molecular Biology.2000
  • 2Lars Ditzel,Jan Lowe,Daniela Stock,Karl-Otto Stetter,Harald Huber,Robert Huber,Stefan Steinbacher.Crystal Structure of the Thermosome,The Archaeal Chaperonin and Homolog of CCT[].Cell.1998
  • 3Iizuka,R,Yoshida,T,Shomura,Y,Miki,K,Maruyama,T,Odaka,M,Yohda,M.ATP binding is critical for the conformational change from an open to closed state in archaeal group II chaperonin[].Journal of Biological Chemistry.2003

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