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Additional resources for Current Protocols in Protein Science: 001
0 with 1 M citric acid. If necessary, remove the butanol layer from the hydrazide gel (from step 3) by aspiration and wash the gel with cold water, then suspend it in 20 ml of cold water. Mix 10 ml of this gel suspension with the oxidized GTP solution and stir the mixture at room temperature for 2 hr. 8 Supplement 29 Current Protocols in Protein Science 6. 8, containing 5 mM EDTA. Retain washings if step 8 is to be performed. Store the resultant GTP-Sepharose at 4°C with an overlay of butanol to retard bacterial growth.
15. Apply the enzyme solution eluted from the above column to a 6 × 2–cm chromatography column packed to 4 cm with GTP-Sepharose 4B, equilibrated with affinity chromatography buffer. Use a flow rate of not more than ∼1 ml/min. 01 (∼150 ml of buffer should be required). 5 ml/min, and this flow rate should be used for step 16. 16. Elute the enzyme activity with a linear 400-ml gradient from 0 to 400 mM KCl in affinity chromatography buffer. Collect fractions (∼10 ml) and monitor the A280 (see Basic Protocol 2), conductivity, and enzyme activity (see Basic Protocol 3) in each.
Not all proteins can fold unassisted by other cellular components. , 1991). The most studied, and just becoming commercially available as of 1995, are the E. coli chaperonins GroEL and GroES, both of which are needed, together with ATP, to renature many proteins. Proline residues can adopt two isomeric conformations in proteins, and the wrong conformation is switched to the correct one by the enzyme prolyl isomerase, aiding the process of protein folding. 2 Purification scheme for insoluble recombinant proteins that are produced as inclusion bodies in the cytoplasm of host cells.