In phi-value analysis, the folding kinetics and conformational folding stability of the wild-type protein are compared with those of one or more point mutants.

Experimental errors can be high in measuring equilibrium stability as well the folding/unfolding rates in water for the wild-type protein and mutants.

The wild-type protein binds to and inhibits trypsin and also the blood protease elastase.

Because endogenous wild-type proteins cannot be visualised in vivo, fusion proteins must be created and their plasmids transfected into the cells studied.

Circularly permuted proteins have been shown to take on different quaternary structure than wild-type proteins.

One method involves the observation of the melting temperature of the wild-type protein versus that of the three mutants.

The transcription and translation machinery of the cell is then in charge of therapy and administers either a wild-type protein or an anti-drug (Fig. 3).

It can be used for affinity chromatography, then used to separate recombinant, overexpressed protein from wild-type protein expressed by the host organism.

A substantial fraction of mutant genomes should be encapsidated with wild-type protein.

Immunofluorescent localization studies showed that this modification had no effect on distribution of the wild-type protein in the cytoplasm (Fig.