Sandbox324: Difference between revisions
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<StructureSection load='4diu' size='340' side='right' caption='Structural Model of Protein 4DIU' scene=''> | <StructureSection load='4diu' size='340' side='right' caption='Structural Model of Protein 4DIU' scene=''> | ||
== Overview of Esterase == | == Overview of Esterase == | ||
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== Proposed Function == | == Proposed Function == | ||
This protein has alpha/beta-hydrolase activity and is of the esterase family. The SPRITE, BLAST, InterPro, and Dali Search along with other bioinformatics analyses consistently matched with carboxylesterases and other esterase-like proteins. SPRITE provided proteins that had similar residues in the active site of the enzyme. SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The isolated protein was introduced to 10 mM p-nitrophenyl acetate in a buffer with a pH of 6. Enzyme activity was measured, and the data was consistent with other hydrolases. | This protein has alpha/beta-hydrolase activity and is of the esterase family. The SPRITE, BLAST, InterPro, and Dali Search along with other bioinformatics analyses consistently matched with carboxylesterases and other esterase-like proteins. SPRITE provided proteins that had similar residues in the active site of the enzyme. Multiple of the matching proteins were esterases and had an RMSD value of <0.5. The RMSD value gives insight into how similar the overlapping sections for the unknown and known proteins are. A value of less than 2 is desired when choosing proteins for reference. SwissDock and Chimera allowed for protein-ligand docking studies. Many of the highlighted interactions were ester-containing ligands and others were susceptible to hydrolysis. The isolated protein was introduced to 10 mM p-nitrophenyl acetate in a buffer with a pH of 6. Enzyme activity was measured, and the data was consistent with other hydrolases. | ||
[[Image:Enzyme_Activity.jpeg]] | [[Image:Enzyme_Activity.jpeg]] | ||
== Structural highlights == | == Structural highlights == | ||
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== References == | == References == | ||
<references/> | <references/> | ||
<ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | |||
