Salvaging the Thermodynamic Destabilization of Interface Histidine in Transmembrane β-Barrels

[Image: see text] The ability of histidine to participate in a wide range of stabilizing polar interactions preferentially populates this residue in functionally important sites of proteins. Histidine possesses an amphiphilic and electrostatic nature that is essential for amino acids residing at mem...

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Detalles Bibliográficos
Autores principales: Iyer, Bharat Ramasubramanian, Vetal, Pallavi Vijay, Noordeen, Henna, Zadafiya, Punit, Mahalakshmi, Radhakrishnan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2018
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6284319/
https://www.ncbi.nlm.nih.gov/pubmed/30284812
http://dx.doi.org/10.1021/acs.biochem.8b00805

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6284319/
https://www.ncbi.nlm.nih.gov/pubmed/30284812
http://dx.doi.org/10.1021/acs.biochem.8b00805

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