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本文引用的文献
1
Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations.
Biophys J. 2007 Oct 1;93(7):2289-99. doi: 10.1529/biophysj.107.105270. Epub 2007 Jun 8.
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Annu Rev Biophys Biomol Struct. 2006;35:115-33. doi: 10.1146/annurev.biophys.35.040405.102010.
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Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations.
Proc Natl Acad Sci U S A. 2006 May 16;103(20):7664-9. doi: 10.1073/pnas.0510426103. Epub 2006 May 8.
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Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis.
Protein Sci. 2006 Jun;15(6):1270-6. doi: 10.1110/ps.062100606. Epub 2006 May 2.
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Coarse-grained normal mode analysis in structural biology.
Curr Opin Struct Biol. 2005 Oct;15(5):586-92. doi: 10.1016/j.sbi.2005.08.007.
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Probing the "annealing" mechanism of GroEL minichaperone using molecular dynamics simulations.
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Structure. 2005 Apr;13(4):565-77. doi: 10.1016/j.str.2005.01.017.
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