Exploring the Cold-Adaptation Mechanism of Serine Hydroxymethyltransferase by Comparative Molecular Dynamics Simulations

Cold-adapted enzymes feature a lower thermostability and higher catalytic activity compared to their warm-active homologues, which are considered as a consequence of increased flexibility of their molecular structures. The complexity of the (thermo)stability-flexibility-activity relationship makes i...

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Detalles Bibliográficos
Autores principales: Zhang, Zhi-Bi, Xia, Yuan-Ling, Dong, Guang-Heng, Fu, Yun-Xin, Liu, Shu-Qun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7916883/
https://www.ncbi.nlm.nih.gov/pubmed/33670090
http://dx.doi.org/10.3390/ijms22041781

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7916883/
https://www.ncbi.nlm.nih.gov/pubmed/33670090
http://dx.doi.org/10.3390/ijms22041781

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