Improving thermostability of papain through structure-based protein engineering.
Choudhury
Debi
D
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata 700064, India.
Biswas
Sampa
S
Roy
Sumana
S
Dattagupta
J K
JK
D001665:Binding Sites; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D016297:Mutagenesis, Site-Directed; D010206:Papain / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D055550:Protein Stability; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013329:Structure-Activity Relationship; D013696:Temperature; D013816:Thermodynamics
D011994:Recombinant Proteins; D003546:Cysteine Endopeptidases; C486917:ervatamin C, Ervatamia coronaria; D010206:Papain