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Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes
A classical model for allosteric regulation of enzyme activity posits an equilibrium between inactive and active conformations. An alternative view is that allosteric activation is achieved by increasing the potential for conformational changes that are essential for catalysis. In the present study,...
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| Pubblicato in: | Protein Sci |
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| Autori principali: | , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
John Wiley and Sons Inc.
2017
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5654843/ https://ncbi.nlm.nih.gov/pubmed/28833948 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.3277 |
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