Heat induces end to end repetitive association in P. furiosusl-asparaginase which enables its thermophilic property

It remains undeciphered how thermophilic enzymes display enhanced stability at elevated temperatures. Taking l-asparaginase from P. furiosus (PfA) as an example, we combined scattering shapes deduced from small-angle X-ray scattering (SAXS) data at increased temperatures with symmetry mates from cry...

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Detalles Bibliográficos
Autores principales: Sharma, Pankaj, Tomar, Rachana, Yadav, Shivpratap Singh, Badmalia, Maulik D., Nath, Samir Kumar, Ashish, Kundu, Bishwajit
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7728782/
https://www.ncbi.nlm.nih.gov/pubmed/33303914
http://dx.doi.org/10.1038/s41598-020-78877-z

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7728782/
https://www.ncbi.nlm.nih.gov/pubmed/33303914
http://dx.doi.org/10.1038/s41598-020-78877-z

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