Room Temperature Phosphoresesnce Study of Refolding of Disulfide Reduced RNase T_1

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Refolding kinetics of distrlfide redtrced ribonttclease T) (RNase Tl ) was stttdied by the recoveryof room teznperatttre phosphorescence emitted f'rouaa a tryptophan residtre (Trp 59) of the protein.When unfolded in a deoxygenated aqueotrs soltrtion, the enzynae does not eraait phosphorescenceat room tetnperattrre, but as soon as the protein was transferred into an anoxic refolding bufl'ersolution, it began enaitting phosphorescence within the mixing dead time (x3O s) of otrr apparatus. The initial quick recovery of RNase Tl phosphorescence was followed by a gradual increasein the phosphorescence lifetime lasting over several tens of' zninutes and then slight decrease to afinal valtre comparable to that of native RNase 'r.. The initial quick recovery o['phosphorescencestrggests that the tryptophan residtre, being exposed to strrrounding water naolectrles when theprotein is trnfolded, is qttickly isolated frona the external water when the enzytne starts refolding,and the gradual change in the phosphorescence lifetirne inuplies that the peptide-chain aroundTrp 59 slowly rearranges itself dtnring the very slow trans-to- cis proline isomerization ?tt Pro 39and/or Pro 55 of the protein.
社団法人日本物理学会の論文
1998-04-15