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Stimulation of the Weak ATPase Activity of Human Hsp90 by a Client…
www-jackson.ch.cam.ac.uk/publications/2002/2002_jmb.pdf15 Sep 2003: Thus, this isthe most stringent test of specicity. The effect ofthe ligand-binding domain of PPAR on the ATPaseactivity of Hsp90 is shown in Figure 3(c). ... This perhaps reects thehigher basal ATPase activity of yeast Hsp90. Perhaps the most stringent -
Review R81 How do small single-domain proteins fold?Sophie E ...
www-jackson.ch.cam.ac.uk/publications/1998/1998_FoldDes.pdf11 Sep 2003: Review R81. How do small single-domain proteins fold?Sophie E Jackson. Many small, monomeric proteins fold with simpletwo-state kinetics and show wide variation in foldingrates, from microseconds to seconds. Thus, stableintermediates are not a -
Mapping the Interactions Present in the Transition State for…
www-jackson.ch.cam.ac.uk/publications/1999/1999_JMB1.pdf15 Sep 2003: Fersht et al. (1994) have proposed akinetic test to distinguish between these possibili-ties. ... This test is based on Brùnsted behaviourobserved in physical organic chemistry for simplesystems in which a single bond is made/broken inthe transition -
Journal of Biological Physics 27: 99–117, 2001.© 2001 Kluwer ...
www-jackson.ch.cam.ac.uk/publications/2001/2001_JBP_Main_et_al.pdf16 Sep 2003: and Fersht, A.R.: Structure of the Hydrophobic Core in the Trans-ition State for Folding of Chymotrypsin Inhibitor 2: A Critical Test of the Protein EngineeringMethod of Analysis. -
Folding Pathway of FKBP12 and Characterisation of the Transition State
www-jackson.ch.cam.ac.uk/publications/1999/1999_JMB2.pdf15 Sep 2003: test whether such an unstable intermediatestate is present on the folding pathway ofFKBP12, refolding experiments were performedin the presence of 0.4 M Na2SO4.
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