PMC:2724026 / 32491-33189 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/2724026","sourcedb":"PMC","sourceid":"2724026","source_url":"https://www.ncbi.nlm.nih.gov/pmc/2724026","text":"Determination of equilibrium stability\nThe stability of WT and mutant proteins was determined using urea-induced equilibrium denaturation followed by fluorimetry using a Cary Eclipse spectrometer (Varian); the excitation wavelength was 280 nm, the emission wavelength was 360 nm and the concentration of protein was ≤ 1–2 μM. The stability of the WT protein was also determined by CD using an Applied Photophysics Chirascan circular dichroism spectropolarimeter; data were collected at 222 nm and the concentration of protein was ≤ 5 μM. All experiments were performed at 25 °C in 50 mM sodium phosphate, pH 7.0, 150 mM NaCl, 5 mM DTT. The data were fit to a two-state transition as described.60,61","divisions":[{"label":"title","span":{"begin":0,"end":38}}],"tracks":[{"project":"2_test","denotations":[{"id":"19362094-3773761-62520552","span":{"begin":696,"end":698},"obj":"3773761"},{"id":"19362094-8476861-62520552","span":{"begin":696,"end":698},"obj":"8476861"}],"attributes":[{"subj":"19362094-3773761-62520552","pred":"source","obj":"2_test"},{"subj":"19362094-8476861-62520552","pred":"source","obj":"2_test"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"2_test","color":"#d1ec93","default":true}]}]}}