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

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

Abstract 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...

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Autores principales: Pankaj Sharma, Rachana Tomar, Shivpratap Singh Yadav, Maulik D. Badmalia, Samir Kumar Nath, Ashish, Bishwajit Kundu
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
Materias:
Medicine
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Science
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Acceso en línea:https://doaj.org/article/cb4ab17049d744219a90d1b286d8a31c
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https://doaj.org/article/cb4ab17049d744219a90d1b286d8a31c

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