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. 2007 Dec 12;82(5):2265–2273. doi: 10.1128/JVI.01641-07

FIG. 7.

FIG. 7.

Renaturation of Det7 tail spike protein. (A) Temperature-sensitive folding. Unfolded Det7tspΔ1-151 protein was diluted 1:400 from 5 M guanidinium chloride at the temperature indicated and allowed to refold and reassemble for 4 days before the formation of detergent-resistant trimers was probed by SDS gel electrophoresis and silver staining. (B) Time course of SDS-resistant trimer formation. Reconstitution of Det7tspΔ1-151 was initiated by a 1:200 dilution from 5 M guanidinium chloride at 4°C. After the times indicated (in hours), trimer reconstitution was quenched by the addition of SDS, followed by SDS-gel electrophoresis.