Punnatin, Panachai <br/><br/>
Molecular dynamics reveals insight into how N226P and H227Y mutations affect maltose binding in the active site of α-glucosidase II from European honeybee, Apis mellifera.  [electronic resource] 

 -  PloS one  2020 
 - e0229734 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1932-6203 
<br/><br/><label>Standard No.: </label>10.1371/journal.pone.0229734  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Substitution<br/>Animals<br/>Bees--enzymology<br/>Catalytic Domain--genetics<br/>Insect Proteins--genetics<br/>Maltose--metabolism<br/>Molecular Dynamics Simulation<br/>Mutation<br/>Protein Binding--genetics<br/>Protein Engineering--methods<br/>Sequence Homology, Amino Acid<br/>Substrate Specificity--genetics<br/>alpha-Glucosidases--genetics