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Folding Pathway of FKBP12 and Characterisation of the Transition State
www-jackson.ch.cam.ac.uk/publications/1999/1999_JMB2.pdf15 Sep 2003: Article No. jmbi.1999.2941 available online at http://www.idealibrary.com on J. Mol. Biol. (1999) 291, 429444. Folding Pathway of FKBP12 and Characterisation ofthe Transition State. Ewan R. G. Main, Kate F. Fulton and Sophie E. Jackson. Cambridge -
doi:10.1016/j.jmb.2007.04.039
www-jackson.ch.cam.ac.uk/publications/2007/2007_J_mol_biol_GFP_unfolding.pdf8 Feb 2008: 19–24 as well as on cooperatively unfoldingregions of proteins.11,14 Although H/D exchangeresults have been reported for GFP, the conditionsused did not allow a quantitative analysis of theresults ... Thesymbols are the same as for (a) except the first -
Folding Study of Venus Reveals a Strong Ion Dependence ...
www-jackson.ch.cam.ac.uk/publications/2010/2010_JBC_Venus_Jackson.pdf8 Feb 2010: pH 8.0 37 CYF 2.22 0.06 5.10 0.01 11.3 0.3 5.11 0.02 8.74 0.04Tyr 1.51 0.07 5.24 -
No Job Name
www-jackson.ch.cam.ac.uk/publications/2006/2006_Khan_JACS_19FGFP.pdf25 Aug 2006: W.Prog. Nucl. Magn. Reson. Spectrosc.1993,. 25, 345-402.(24) Kaptein, R.Bio. Magn. Reson.1982, 4, 145-91.(25) Kaptein, R.; Dijkstra, K.; Nicolay, K.Nature 1978, 274, -
Ubiquitin folds through a highly polarizedtransition state Heather…
www-jackson.ch.cam.ac.uk/publications/2005/2005_PEDS_Ubiquitin_Went_Jackson.pdf6 Sep 2005: 0.04 4.46 6 0.07 0.50 6 0.03 1.24 6 0.01 4.22 6 0.07 2.74 6 0.07Ile!Val23 0.45 6 ... 0.04 5.54 6 0.10 0.57 6 0.04 1.24 6 0.02 5.18 6 0.08 2.74 6 0.07Ile!Ala23 2.78 6 -
doi:10.1016/j.jmb.2006.04.032
www-jackson.ch.cam.ac.uk/publications/2006/2006_Mallam_JMB_YibK.pdf4 Jul 2006: Double-jump unfolding experiments wereused to detect faster unfolding phases corres-ponding to non-native species populated on therefolding pathway.24–26 In these experiments,refolding was allowed for short amounts ... 0.940.10 0.250.02 1.20.1 -
b908170b 2951..2965
www-jackson.ch.cam.ac.uk/publications/2009/2009_Hsu_ChemRev.pdf28 Sep 2009: pH 6.0 at 25 1C as a function of equilibration time: from right to left 3 h, 12 h, 24 h, 48 h, 5 days, 13 days, 44 days (adapted ... group to demonstrate how information on protein structure. can be obtained using a mechanical triangulation technique.24. -
doi:10.1016/j.jmb.2005.11.085
www-jackson.ch.cam.ac.uk/publications/2006/2006_McLaughlin_JMB_Hsp90.pdf21 Apr 2006: p23appears to stabilise the interaction between Hsp90and a client protein in vitro,23,24 correlating with itsability to increase the activation of heterologouslyexpressed estrogen receptor in vivo.25 In contrast,another -
doi:10.1016/j.jmb.2004.05.007
www-jackson.ch.cam.ac.uk/publications/2004/2004_JMB_Hsp90_Zhang_et_al.pdf23 Aug 2004: However, it stronglyinhibits the ATPase activity in the presence of aclient-protein.10 Recent work has shown that Sti1/Hop binds to the first 24 amino acid residues ofHsp90 thereby preventing ... N terminus ofHsp90 is within the first 24 amino acid -
doi:10.1016/j.jmb.2006.11.014
www-jackson.ch.cam.ac.uk/publications/2007/2007_J_mol_biol_YbeA+YibK.pdf8 Feb 2008: topology that led to the hypothesisthat topology, not sequence, is the major contribut-ing factor in how a protein folds.23,24 If proteinfolding rates and mechanisms are determinedlargely by the
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