Explanipedia

De novo design of allosterically switchable protein assemblies Open

Arvind Pillai, Abbas Idris, Annika Philomin, Connor Weidle, Rebecca Skotheim , et al. · 2024

Allosteric modulation of protein function, wherein the binding of an effector to a protein triggers conformational changes at distant functional sites, plays a central part in the control of metabolism and cell signalling^1-3. Th…

De novo design of allosterically switchable protein assemblies Open

Arvind Pillai, Abbas Idris, Annika Philomin, Connor Weidle, Rebecca Skotheim , et al. · 2023

Allosteric modulation of protein function, wherein the binding of an effector to a protein triggers conformational changes at distant functional sites, plays a central role in the control of metabolism and cell signaling 1–3 . There has be…

Design of stimulus-responsive two-state hinge proteins Open

Florian Praetorius, Philip J. Y. Leung, Maxx H. Tessmer, Adam Broerman, Cullen Demakis , et al. · 2023

In nature, proteins that switch between two conformations in response to environmental stimuli structurally transduce biochemical information in a manner analogous to how transistors control information flow in computing devices. Designing…

Data for: Design of stimulus-responsive two-state hinge proteins Open

Florian Praetorius, Philip J. Y. Leung, Maxx H. Tessmer, Adam Broerman, Cullen Demakis , et al. · 2023

Supplementary information for Design of stimulus-responsive two-state hinge proteins: Design scripts, design models, and aw DEER data.

Data for: Design of stimulus-responsive two-state hinge proteins Open

Florian Praetorius, Philip J. Y. Leung, Maxx H. Tessmer, Adam Broerman, Cullen Demakis , et al. · 2023

Supplementary information for Design of stimulus-responsive two-state hinge proteins: Design scripts, design models, and aw DEER data.

Design of stimulus-responsive two-state hinge proteins Open

Florian Praetorius, Philip J. Y. Leung, Maxx H. Tessmer, Adam Broerman, Cullen Demakis , et al. · 2023

Proteins that switch between two structural states as a function of environmental stimuli are widespread in nature. These proteins structurally transduce biochemical information in a manner analogous to how transistors control information …

Conserved patterns and interactions in the unfolding transition state across <span>SH3</span> domain structural homologues Open

Cullen Demakis, Matthew C. Childers, Valerie Daggett · 2020

Proteins with similar structures are generally assumed to arise from similar sequences. However, there are more cases than not where this is not true. The dogma is that sequence determines structure; how, then, can very different sequences…

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