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Refolded proteins, thermostability

Thermostability of Drifted Oligomeric, Reduced, and Refolded Proteins... [Pg.64]

The fastest-folding small proteins generally fold on much slower time scales than the time scale of formation of secondary structure. The speed record is currently held by lambda(6-85), a truncated, monomeric form of the N-terminal domain of lambda repressor, which refolds with a half-life of approximately 140 fjis. A thermostable lambda(6-85) variant with alanine substituted for glycine residues 46 and 48 in the third helix folds faster in dilute solutions of de-naturant, with an extrapolated half-life of less than 10 /us in water.13 Cold-shock protein CspB from Bacillus subtilis folds in about 1 ms.61 Engineered mutants of the P22 Arc repressor62 and CI263 fold in a fraction of a millisecond. [Pg.297]


See other pages where Refolded proteins, thermostability is mentioned: [Pg.195]    [Pg.180]    [Pg.52]    [Pg.436]    [Pg.190]    [Pg.153]    [Pg.341]    [Pg.48]    [Pg.193]   
See also in sourсe #XX -- [ Pg.64 , Pg.65 , Pg.66 , Pg.67 , Pg.68 , Pg.69 , Pg.70 , Pg.71 , Pg.72 , Pg.73 , Pg.74 , Pg.75 , Pg.76 ]




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