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Temperature, stability, and the hydrophobic interaction.
Changes in free energy are normally used to track the effect of temperature on the stability of proteins and hydrophobic interactions. Use of this procedure on the aqueous solubility of hydrocarbons, a standard representation of the hydrophobic effect, leads to the conclusion that the hydrophobic ef...
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| Hovedforfatter: | |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
1997
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1181201/ https://ncbi.nlm.nih.gov/pubmed/9414210 |
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