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A fluorescence stopped-flow kinetic study of the conformational activation of α-chymotrypsin and several mutants
The kinetic activation parameters (activation free energy, activation free enthalpy, and activation free entropy change) of the conformational change of α-chymotrypsin from an inactive to the active conformation were determined after a pH jump from pH 11.0 to pH 6.8 by the fluorescence stopped-flow...
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| Autori principali: | , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Cold Spring Harbor Laboratory Press
2004
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2280002/ https://ncbi.nlm.nih.gov/pubmed/15322291 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.04709604 |
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