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The significance of denaturant titrations of protein stability: a comparison of rat and baker's yeast cytochrome c and their site-directed asparagine-52-to-isoleucine mutants.
The residue asparagine-52 of rat cytochrome c and baker's yeast iso-1-cytochrome c was mutated to isoleucine by site-directed mutagenesis, and the unfolding of the wild-type and mutant proteins in urea or guanidinium chloride solutions was studied. Whereas the yeast mutant cytochrome unfolded i...
Sparad:
| Huvudupphovsmän: | , , , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
1994
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1138278/ https://ncbi.nlm.nih.gov/pubmed/8172593 |
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