Sandbox Reserved 1846: Difference between revisions
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The WCCG variant (F243W/D238C/S283C/Y127G) had specific activity slightly lower than ICCG, but showed even greater thermostability, with a melting temperature increase of +10.1°C. It reached 90% PET depolymerization in 10.5 hours at 72°C.<ref name="Tournier"/> | The WCCG variant (F243W/D238C/S283C/Y127G) had specific activity slightly lower than ICCG, but showed even greater thermostability, with a melting temperature increase of +10.1°C. It reached 90% PET depolymerization in 10.5 hours at 72°C.<ref name="Tournier"/> | ||
Other stabilizing mutations, such as T96M, N246D, and N246M, were also tested, but excluded as they were not part of the top-performing mutant (ICCG) | Other stabilizing mutations, such as T96M, N246D, and N246M, were also tested, but excluded as they were not part of the top-performing multi-mutant variant (ICCG).<ref name="Tournier"/> | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
A binding model of the substrate 2-HE(MHET)3 in wild-type | A binding model of the substrate 2-HE(MHET)3 in wild-type LCC (4eb0.pdb) was constructed and refined to mimic the 3D structure illustrated in Figure 2 of reference <ref name="Tournier"/>. The software Maestro (Schrödinger, Inc; version 14.2.118) was used to construct the initial binding structure, followed by energy minimization in the context of the rigid protein that had previously been processed to add/refine all hydrogen atoms. The ligand model was then used without further modification to identify and illustrate the cited active-site residues.<references/> | ||
== Student Contributors == | == Student Contributors == | ||
Ashley Callaghan, Rebecca Hoff, & Simone McCowan | Ashley Callaghan, Rebecca Hoff, & Simone McCowan | ||
