S. Marqusee

This study investigates how circular permutation affects protein folding and aggregation in HaloTag, finding that termini placement in flexible regions is more critical than proteostasis factors.

The paper proposes a step-wise activation model for metabotropic glutamate receptor subtype 5, supported by structural and fluorescence imaging data of different activation states.

The paper compares consensus and ancestral protein reconstruction methods using Ribonuclease H sequences, finding that phylogenetically restricted consensus proteins are more stable than those from diverse clades.

The paper uses nanopore sequencing to study the single-nucleotide kinetics of a reverse transcriptase, revealing its ability to sense and destabilize RNA structures during cDNA synthesis.

The paper identifies a conserved neutralizing epitope on the S2 domain of SARS-CoV, SARS-CoV-2, and MERS-CoV spike proteins that is targeted by antibody 3A3.

The paper identifies ultrapotent SARS-CoV-2-neutralizing nanobodies that bind a conserved epitope on the spike protein, showing therapeutic efficacy in hamsters.

The paper identifies a Switch-Helix in eIF2B that allosterically regulates ISR signaling and is conserved across species.

This study shows RAMP2 inhibits GCGR signaling by inducing conformational changes and disorder in the receptor's extracellular domain.

The paper identifies a mutation in S100A9 that stabilizes a non-functional conformation, revealing an evolutionary constraint on stabilizing mutations.

The paper generates a bacterial-expressible Syk-family kinase via ancestral sequence reconstruction and uses deep mutational scanning to identify functional mutations.

This study shows that cancer hotspot mutations in Ras activate it regardless of stability, while non-hotspot mutations can be activating or deleterious depending on stability.

This study uses HDX/MS to show ligand-induced changes in dynamics mediate long-range allostery in the lac repressor, revealing flexibility differences in secondary structures across functional states.

This study evaluates how rigid DNA nanotube tethers affect noise in dual-trap optical tweezers systems, finding they suppress high-frequency noise but not low-frequency noise.

This study compares the conformational dynamics of the tandem-SH2 modules in Syk and ZAP-70 kinases, revealing differences in their autoinhibited states and activation mechanisms.

The paper identifies an alternative open-trimer conformation of the SARS-CoV-2 spike ectodomain that exposes novel epitopes and is modulated by temperature, binding, and sequence variants.

This study investigates how ubiquitination at different sites affects the energy landscape of a model protein, revealing distinct thermodynamic mechanisms for destabilization and protection.

This study investigates how sequence variation in the alpha-lytic protease family relates to kinetic stability and energy landscapes, finding that pro-region size and specific amino acids influence folding speed and stability.

The paper uses single-molecule techniques to show catalysis does not enhance diffusion of alkaline phosphatase, contradicting previous FCS results attributed to substrate-induced dye blinking.

This study investigates how the ribosome affects the folding and unfolding of RNase H during translation, finding that ribosome-stalled RNase H unfolds faster but maintains the same folding rate.

This study shows that ubiquitination at specific sites destabilizes protein structure and enhances proteasomal degradation, even in well-folded proteins.

The paper identifies CsoS2's N-terminal peptide as a multivalent interaction hub that binds Rubisco through electrostatic interactions, enabling efficient α-carboxysome formation via avidity.

This study investigates long-range energetic coupling in T4 lysozyme by analyzing a circularly permuted variant, showing that helix stabilization enhances subdomain stability through salt bridge interactions.

This study shows the src SH3 domain folds through the same pathway whether on or off the ribosome, suggesting the ribosome does not alter its folding mechanism.

This study uses ancestral sequence reconstruction and hydrogen exchange to trace the folding pathway of RNase H across evolutionary time, finding conserved intermediates but divergent pathways.