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Thermodynamic characterization of an equilibrium folding intermediate of staphylococcal nuclease.
High-sensitivity differential scanning calorimetry and CD spectroscopy have been used to probe the structural stability and measure the folding/unfolding thermodynamics of a Pro117-->Gly variant of staphylococcal nuclease. It is shown that at neutral pH the thermal denaturation of this protein is...
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| Huvudupphovsmän: | , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
Cold Spring Harbor Laboratory Press
1994
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2142756/ https://ncbi.nlm.nih.gov/pubmed/7756977 |
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