Title : Kinetic folding studies of the P22 tailspike beta-helix domain reveal multiple unfolded states.

Pub. Date : 2009 May

PMID : 19258192






1 Functional Relationships(s)
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1 The slow refolding step could be partly attributed to proline isomerization, based on an increased rate during refolding in the presence of PPIase and an increased relative amplitude of this step with increasing delay time in double-jump refolding experiments observed over delays of 5-100 s. However, double-jump refolding experiments with delay times longer than 100 s along with size exclusion chromatography and dynamic light scattering of refolding samples showed that the overall refolding yield decreased as bhx was unfolded for longer periods of time. Proline FKBP prolyl isomerase 1B Homo sapiens