Evaluation of irreversible protein thermal inactivation caused by breakage of disulphide bonds using methanethiosulphonate

Many extracellular globular proteins have evolved to possess disulphide bonds in their native conformations, which aids in thermodynamic stabilisation. However, disulphide bond breakage by heating leads to irreversible protein denaturation through disulphide-thiol exchange reactions. In this study,...

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Detalles Bibliográficos
Autores principales: Futami, Junichiro, Miyamoto, Ai, Hagimoto, Atsushi, Suzuki, Shigeyuki, Futami, Midori, Tada, Hiroko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5622167/
https://www.ncbi.nlm.nih.gov/pubmed/28963503
http://dx.doi.org/10.1038/s41598-017-12748-y

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5622167/
https://www.ncbi.nlm.nih.gov/pubmed/28963503
http://dx.doi.org/10.1038/s41598-017-12748-y

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