Molecular mechanism for thermal denaturation of thermophilic rhodopsin
نویسندگان
چکیده
منابع مشابه
Mechanism of thermal denaturation of maltodextrin phosphorylase from Escherichia coli.
Maltodextrin phosphorylase from Escherichia coli (MalP) is a dimeric protein in which each approximately 90-kDa subunit contains active-site pyridoxal 5'-phosphate. To unravel factors contributing to the stability of MalP, thermal denaturations of wild-type MalP and a thermostable active-site mutant (Asn-133-->Ala) were compared by monitoring enzyme activity, cofactor dissociation, secondary st...
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ژورنال
عنوان ژورنال: Chemical Science
سال: 2019
ISSN: 2041-6520,2041-6539
DOI: 10.1039/c9sc00855a