Results 131 to 140 of about 114,766 (235)

Protein Structuromics Reveals a Loop‐Controlled Half‐Open Active Pocket Conformation Throughout Fe(II)/α‐ketoglutarate‐Dependent Dioxygenase Catalytic Cycle

open access: yesAdvanced Science, EarlyView.
This study reveals a conserved half‐open active pocket in Fe(II)/α‐ketoglutarate‐dependent dioxygenases through protein structuromics, distinguished by structural features comprising highly flexible loop elements. Enhanced sampling simulations‐guided mutagenesis experiments elucidated how this flexible loop regulates pocket open/closed conformations ...
Lunjie Wu   +10 more
wiley   +1 more source

SuFEx‐Enabled Reprogramming of Flavonoids for Selective α‐Glucosidase Covalent Inhibition

open access: yesAdvanced Science, EarlyView.
Selective inhibition of intestinal α‐glucosidase remains limited by poor enzyme specificity and off‐target metabolic effects. Here, SuFEx click chemistry is used to reprogram natural flavonoids into covalent inhibitors with enhanced α‐glucosidase selectivity and controlled reactivity. This strategy enables effective regulation of carbohydrate digestion
Fengyu Guo   +14 more
wiley   +1 more source

High Free‐Volume Imidazole‐Based Ionomers for High‐Temperature Proton Exchange Membrane Fuel Cells

open access: yesAdvanced Science, EarlyView.
High free‐volume imidazole‐based ionomers (PF4IM‐72) enable enhanced phosphoric acid uptake and efficient proton transport, delivering peak power densities of 0.645 W cm−2 at 160 °C and 0.838 W cm−2 at 200 °C in HT‐PEMFCs. This work highlights a promising platform for next‐generation ionomers with improved high‐temperature performance and stability ...
Ge Chao   +7 more
wiley   +1 more source

Intramolecular Interactions between Folded and Disordered Regions Shape Ubiquilin Structure and Function

open access: yesAdvanced Science, EarlyView.
Ubiquilin (UBQLN), like many other human proteins, contains both well‐folded and disordered regions. Here, we show that intramolecular interactions between disordered regions and folded domains modulate between open and closed topologies of UBQLN proteins, altering their structure and function.
Jessica K. Niblo   +4 more
wiley   +1 more source

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