mutant protein

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Long before mutant proteins could be created in the laboratory, he had a large collection of single-site mutants of haemoglobin.
Similarly, when transfected into living epithelial cells, the mutant proteins behaved abnormally.
For this reason, the spectra of mutant proteins have to be evaluated very carefully.
The unstable or partially folded mutantprotein does not undergo trafficking and is usually rapidly degraded.
The mutantprotein lacks the cytoplasmic region, and is likely to be defective in signal transduction.
It is possible that the differences seen reflect the different genetic background of the families concerned, rather than functional differences in the mutantprotein itself.
The mutantprotein was unable to form intermediate filaments in vitro or intermediate filament networks in cultured muscle cells.
One possibility is that the chaperone capacity of a-crystallin is overwhelmed by the large amount of mutantprotein.
This experiment suggests that removal or inactivation of the mutantprotein might be an effective therapeutic strategy, even after the onset of clinical disease.
However, in all cases, a significant proportion of the mutantprotein formed disulphide-bonded dimers and higher molecular weight aggregates.
Perhaps substitution of the proline residue in the mutantprotein results in misfolding of the protein and degradation prior to insertion into the plasma membrane.
Therefore, one approach to promote folding of processing mutants would be to stabilise the mutant protein during the folding process through the use of chemical chaperones.
A mutation that leads to a mutantprotein that disrupts the activity of the wild-type protein in the multimer is a dominant-negative mutation.
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