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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: The IC50 is approximately 10 mM (data notshown) similar to that measured for yeast Hsp90.24. ... J. Biol. Chem. 274, 17525-17533. 24. Panaretou, B., Prodromou, C., Roe, S. -
Folding and stability of the ligand-bindingdomain of the…
www-jackson.ch.cam.ac.uk/publications/2002/2002_prot_sci.pdf17 Sep 2003: Sci.24: 136–141. Chen, S., Prapapanich, V., Rimerman, R.A., Honore, B., and Smith, D.F. -
doi:10.1016/j.bpc.2004.05.009
www-jackson.ch.cam.ac.uk/publications/2004/2004_Biophys_Chem_UBQ_Mariana.pdf23 Aug 2004: Received 24 March 2004; received in revised form 14 May 2004; accepted 17 May 2004. ... 24] within the GROMACS software package. This. method divides the conformational space of the protein. -
doi:10.1016/j.jmb.2004.12.055
www-jackson.ch.cam.ac.uk/publications/2005/2005_Mallam_JMB_KnottedPortein.pdf17 Jul 2005: This observation is notexpected for a simple two-state denaturation mech-anism, and indicates that a more complex scheme isnecessary to describe the system fully.24,25 In particu-lar, the ... transition is biphasic33–37 and each transition can -
Evidence of an Intermediate and Parallel Pathways in ProteinUnfolding …
www-jackson.ch.cam.ac.uk/publications/2008/2008_JACS_SM_GFP.pdf1 Aug 2008: AM. CHEM. SOC. 2008, 130, 7898–7907. identified as a continuum-of-substates,19 expansion or collapseof the unfolded state,18,23,24 or just assigned to changes in thedye’s ... Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 11539–11543. (24) Hoffmann, A.; -
Mapping the Interactions Present in the Transition State for…
www-jackson.ch.cam.ac.uk/publications/1999/1999_JMB1.pdf15 Sep 2003: Ala75 2.6 0.11 ÿ5.51 0.12 1.01 0.02 ÿ1.55 0.04 0.34 0.03 0.24 0.01Thr! ... Val76 0.76 0.12 ÿ7.90 0.12 0.94 0.02 ÿ4.24 0.05 0.56 0.2 0.43 0.09Ile! -
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 -
Protein folding: Defining a “standard” set ofexperimental conditions…
www-jackson.ch.cam.ac.uk/publications/2005/2005_Maxwell_ProSci_proteinfolding.pdf19 Apr 2005: Forexample, 13 of the proteins characterized here were in-cluded in an earlier 24-protein data set that was used toillustrate the relationship between an empirical measure oftopology termed relative contact ... 07 2.04 0.03 13.0 1.9 4.2 0.5 -
Knot formation in newly translated proteins is spontaneous and…
www-jackson.ch.cam.ac.uk/publications/2012/2012_Nat_Chem_Biol_Knots_GroEL.pdf13 Jan 2012: coli 0 4.7 0.1 2.9 0.1 21.8 0.5 –. 1.0 5.5 0.1 24.1 0.6 21 9In vitro expression in a ... pulse proteolysis and western blotting. Protein Sci. 18, 1051–1059 (2009).24. Park, C. & -
doi:10.1016/j.str.2006.11.007
www-jackson.ch.cam.ac.uk/publications/2007/2007_structure_YibK.pdf8 Feb 2008: Sextuple 2.6 ( 0.4) 3 102 2.0 ( 0.6) 3 103 0.24 0.07 0.33 0.03 0.6 0.1 1.5 0.3. -
The extremely slow-exchanging core andacid-denatured state of green…
www-jackson.ch.cam.ac.uk/publications/2008/2008_HFSP_J_GFP.pdf19 Dec 2008: Neuberger, A (ed.), pp 23–24,Methuen, London. Mayo, SL, and Baldwin, RL (1993). -
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 -
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.2004.09.055
www-jackson.ch.cam.ac.uk/publications/2004/2004_JMB_McLaughlin_Hsp90.pdf6 Jan 2005: Trends Biochem. Sci. 25,24–28. 17. Weikl, T., Muschler, P., Richter, K., Veit, T., Reinstein, J.& Buchner, J. ... J. Biol. Chem. 275, 37181–37186. 24. Adair, G. S. (1925). The hemoglobin system. -
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 -
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 -
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. -
No Job Name
www-jackson.ch.cam.ac.uk/publications/2004/2004_Biochemistry_UBQ_core.pdf23 Aug 2004: Wild-type and mutant proteins wereexpressed and purified as described elsewhere (24-25). ... Struct. Biol. 8, 331-333. 24. Finucane, M. D., Tuna, M., Lees, J. -
Local and long-range stability in tandemly arrayedtetratricopeptide…
www-jackson.ch.cam.ac.uk/publications/2005/2005_PNAS_Main_tetratricopeptide.pdf17 Jul 2005: first 24 h, then the number of scans wasdoubled, and data were collected over the next 5– 40 days. ... 1 T kin† T eq.‡. CTPR2 19,860 6,692 50 2.24 0.19 0.35 0.21 2.06 0.18 0.5 0.4CTPR3 35,032 7,601 -
Review R81 How do small single-domain proteins fold?Sophie E ...
www-jackson.ch.cam.ac.uk/publications/1998/1998_FoldDes.pdf11 Sep 2003: given here is twice that of the monomer [23]. mInitial reports suggested that wild-type ubiquitin folded with two-state kinetics [24]. ... 4]), activation domain procarboxypeptidase (ADAh2; [22]), ubiquitin[24,25], histidine-containing phosphocarrier
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