Thermodynamics of protein denaturation at temperatures over 100 °C: CutA1 mutant proteins substituted with hydrophobic and charged residues

Although the thermodynamics of protein denaturation at temperatures over 100 °C is essential for the rational design of highly stable proteins, it is not understood well because of the associated technical difficulties. We designed certain hydrophobic mutant proteins of CutA1 from Escherichia coli,...

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Detalles Bibliográficos
Autores principales: Matsuura, Yoshinori, Takehira, Michiyo, Joti, Yasumasa, Ogasahara, Kyoko, Tanaka, Tomoyuki, Ono, Naoko, Kunishima, Naoki, Yutani, Katsuhide
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4620440/
https://www.ncbi.nlm.nih.gov/pubmed/26497062
http://dx.doi.org/10.1038/srep15545

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4620440/
https://www.ncbi.nlm.nih.gov/pubmed/26497062
http://dx.doi.org/10.1038/srep15545

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