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The conformations of the enzyme cyclophilin A that are essential for its catalytic activity are temperature dependent and exhibit diverse responses, which is consistent with a complex energy landscape.

Molecular simulations can capture key aspects of the conformational exchange in a protein.

The conformational dynamics of multidrug resistance protein 1 (MRP1) are tracked in real time by single-molecule fluorescence resonance energy transfer experiments, which elucidate the rate-limiting mechanism of MRP1's transport cycle.

SARS-CoV-2 entry mechanism through membrane fusion is regulated by the spike protein glycosylation state.

Multimodal spectroscopy (smFRET, EPR, SAXS, and SANS) and integrative structural modeling reveal large-scale domain rearrangements in human guanylate binding protein 1 (hGBP1) that are driving forces for the formation of oligomers that enable its biological function in innate immune defense.

We are writing to comment on the article by El Hage et al., 2018 about molecular dynamics simulations of human hemoglobin.

Computational methods reveal how mutations affect the conformational landscape of the kinase domain of EGFR resulting in abnormal signaling and provide a structural framework for ongoing drug discovery efforts on mutant-specific EGFR inhibition.

Structures of a transition metal transporter spanning the entire Mn²⁺ transport cycle reveal distinct coordination geometries and dynamic polar networks that enable Mn²⁺ import, and a Cd²⁺-bound structure helps explain how Cd²⁺ behaves differently as a substrate.

Specific and non-specific conformational confinement, via point mutation or cochaperone interaction or macro-molecular crowding, stimulates protein function in Hsp90 by reducing non-productive conformational flexibility.

Single-turnover studies reveal quantitative insights into the inner mechanics and unfold hidden facets in the conformational coupling of ATP binding, hydrolysis, and substrate translocation by ABC transporters.