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2017 | 1 |
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Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.
Protein Sci. 2017 Nov;26(11):2221-2228. doi: 10.1002/pro.3277. Epub 2017 Sep 30.
Protein Sci. 2017.
PMID: 28833948
Free PMC article.
Random circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and function.
Beernink PT, Yang YR, Graf R, King DS, Shah SS, Schachman HK.
Beernink PT, et al.
Protein Sci. 2001 Mar;10(3):528-37. doi: 10.1110/ps.39001.
Protein Sci. 2001.
PMID: 11344321
Free PMC article.
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