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doi:10.1016/j.bpc.2007.03.011
www-jackson.ch.cam.ac.uk/publications/2007/2007_biophys_chem_UBQ.pdf8 Feb 2008: a linear, additive fashion[16,17], with typical increases in stability of around 1–2 kcal/mol in 200–300 g/L of cosolute [16,18–22]. ... Examination ofdestabilised mutants of ubiquitin here confirms this hypothesis,with an increase around 1.2 -
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: at pH 7.5 in a buffer containing 200 mM KCl and10% (v/v) glycerol. ... Conditions: 25 C, 50 mM Tris–HCl(pH 7.5), 200 mM KCl, 10% (v/v) glycerol, 1 mM DTT. -
doi:10.1016/j.jmb.2007.04.059
www-jackson.ch.cam.ac.uk/publications/2007/2007_J_mol_biol_Hsp90+co.pdf8 Feb 2008: Forlocalisation of hydrogen exchange in pepsin-digestedHsp90 samples, typical instrumental settings include:mass range 200–2000 Da, capillary voltage 1400 V andcone voltage 20 V. -
doi:10.1016/j.jmb.2007.06.065
www-jackson.ch.cam.ac.uk/publications/2007/2007_J_mol_biol_Hsp90_inhibition.pdf8 Feb 2008: A 200 μl sampleof 20 μM DMAG was injected into a 1.4 ml cell containing1 μM wild-type Hsp90. -
doi:10.1016/j.jmb.2008.02.013
www-jackson.ch.cam.ac.uk/publications/2008/2008_JMB_Hsp90_Hop.pdf4 Jun 2008: Bound protein was eluted witha linear salt gradient over 200 mL from 0 to 2 M NaCl.Protein was further purified by gel-filtration chromato-graphy on either a G75 Sepharose ... Protein interaction assays. Protein interaction was assayed according to -
doi:10.1016/j.molcel.2008.03.019
www-jackson.ch.cam.ac.uk/publications/2008/2008_Mol_Cell_Knotted_Fusions.pdf1 Aug 2008: from the amino terminus, as the threading of an Escherichia. coli ribosome (approximately 200 Å in diameter [Schuwirth. ... 50 mM Tris-HCl (pH 7.5), 200 mM KCl, 10 % (v/v) glycerol, and 1 mM DTT at. -
doi:10.1016/j.str.2006.11.007
www-jackson.ch.cam.ac.uk/publications/2007/2007_structure_YibK.pdf8 Feb 2008: 225 nm. Conditions: 25C in 50 mM Tris-HCl. (pH 7.5), 200 mM KCl, 10% (v/v) glycerol,. ... 200 mM KCl, 10 % glycerol (v/v), 1 mM DTT, except for the ITC exper-. -
doi:10.1016/j.str.2008.04.004
www-jackson.ch.cam.ac.uk/publications/2008/2008_Structure_Jackson_commentary.pdf1 Aug 2008: Structure 16, May 200. to be a compact state in which the N-ter-. ... require large quantities of stable and. homogeneous species. Structure 16, May 200. -
Exploring knotting mechanisms in protein foldingAnna L. Mallam,…
www-jackson.ch.cam.ac.uk/publications/2008/2008_PNAS_YibK_mutants.pdf8 Dec 2008: All experiments were performed in abuffer of 50 mM TrisHCl (pH 7.5), 200 mM KCl, 10% glycerol (vol/vol), 1 mMDTT, except for ITC experiments where -mercaptoethanol replaced DTT asthe
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