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Reusable SERS active substrates for ultrasensitive molecular detection
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Structural Insights into WD-Repeat 48 Activation of Ubiquitin-Specific Protease 46
Abstract not provided
Perturbation of the Conformational Dynamics of an Active-Site Loop Alters Enzyme Activity
The role of internal dynamics in enzyme function is highly debated. Specifically, how small changes in structure far away from the reaction site alter protein dynamics and overall enzyme mechanisms is of wide interest in protein engineering. Using RNase A as a model, we demonstrate that elimination of a single methyl group located >10 Å away from the reaction site significantly alters conformational integrity and binding properties of the enzyme. This A109G mutation does not perturb structure or thermodynamic stability, both in the apo and ligand-bound states. However, significant enhancement in conformational dynamics was observed for the bound variant, as probed over nano- to millisecond timescales, resulting in major ligand repositioning. Furthermore, these results illustrate the large effects caused by small changes in structure on long-range conformational dynamics and ligand specificities within proteins, further supporting the importance of preserving wild-type dynamics in enzyme systems that rely on flexibility for function.
Molecular Understanding of USP7 Substrate Recognition and C-Terminal Activation
Abstract not provided
Dual Site Phosphorylation of Caspase-7 by PAK2 Blocks Apoptotic Activity by Two Distinct Mechanisms
Not Available
Trypanosomatid Deoxyhypusine Synthase Activity Is Dependent on Shared Active-Site Complementation between Pseudoenzyme Paralogs
Abstract not provided
Identification of Radiolytically-Active Thermal Transition Phases in Boehmite
Abstract not provided