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Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.
Rational design of a monomeric and photostable far-red fluorescent protein for fluorescence imaging in vivo.
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.
Subunit interface mutants of rabbit muscle aldolase form active dimers.