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Showing 1–11 of 11 results
Advanced filters: Author: Jason D. Galpin Clear advanced filters

  • Fast inactivation is characteristic of voltage-gated sodium channels. In this work, the authors show that this process occurs in two distinct, consecutive steps and propose a lock and key model for fast inactivation.

    • Yichen Liu
    • Jason D. Galpin
    • Francisco Bezanilla
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-13

  • The authors identify a single main-chain hydrogen bond required to keep GABAA receptors closed in the absence of neurotransmitter. Electrophysiology and molecular dynamics simulations suggest disruption of this bond is a key component of channel opening during inhibitory synaptic signaling in the brain.

    • Cecilia M. Borghese
    • Jason D. Galpin
    • Marcel P. Goldschen-Ohm
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-10

  • Binding-activated optical sensors are powerful tools, but their development can be slow and laborious. Here, authors introduce a platform to expedite biosensor discovery and evolution using genetically encodable fluorogenic amino acids.

    • Erkin Kuru
    • Jonathan Rittichier
    • George M. Church
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-14

  • CLC-type channels selectively transport Cl− across biological membranes, but it is unclear how discrimination between anions is maintained. Here, authors use a combination of non-natural amino acid substitutions, electrophysiology, and molecular dynamics simulations to determine Cl− specificity within this family of ion channels.

    • Lilia Leisle
    • Kin Lam
    • Alessio Accardi
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-11

  • Aromatic amino acids in proteins support ligand binding and protein stability. To parse the physiocochemical roles of aromatic interactions, here Galles, Infield and co-authors identify pyrrolysine-based aminoacyl-tRNA synthetases that enable the encoding of fluorinated phenylalanine amino acids.

    • Grace D. Galles
    • Daniel T. Infield
    • Christopher A. Ahern
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-12

  • Class I anti-arrhythmic drugs act at cardiac sodium channels and are subdivided into classes Ia-c based on their effects on the electrocardiogram. Here, class Ib drugs are found to rely on cation–pi interactions for their activity, whereas class Ib and Ic drugs rely significantly less on this interaction.

    • Stephan A. Pless
    • Jason D. Galpin
    • Christopher A. Ahern
    Research
    Nature Communications
    Volume: 2, P: 1-9

  • Voltage-gated potassium channels cycle between closed and open states through poorly-defined transitions. Pless and colleagues incorporate artificial amino acids into Shaker potassium channels and find that that the negative electrostatic surface potential of Phe481, destabilizes the channel open state.

    • Stephan A. Pless
    • Ana P. Niciforovic
    • Christopher A. Ahern
    ResearchOpen Access
    Nature Communications
    Volume: 4, P: 1-11

  • The antiepileptic drug retigabine potentiates neuronal KCNQ potassium channels. Here, the authors use a combination of unnatural amino acid mutagenesis and electrophysiology to show that retigabine acts by hydrogen bonding with a tryptophan indole nitrogen in the channel pore.

    • Robin Y. Kim
    • Michael C. Yau
    • Harley T. Kurata
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-11

  • Salt bridges between positively charged residues within the S4 transmembrane segment of the voltage-sensing potassium channel, Shaker, and acidic residues in S2 and S3 segments are not necessary during channel gating; rather, two of the acidic residues may occupy a hydrophilic water-filled vestibule that creates an energetically favorable environment for S4 movement during channel gating.

    • Stephan A Pless
    • Jason D Galpin
    • Christopher A Ahern
    Research
    Nature Chemical Biology
    Volume: 7, P: 617-623

  • The helical transmembrane segments of membrane proteins play central roles in sensory transduction but the mechanistic basis for their function remains unresolved. Here the authors identify regions in the S4 voltage-sensing segment of Shaker potassium channels where local helical structure is reliant upon backbone amide support.

    • Daniel T. Infield
    • Kimberly Matulef
    • Francis I. Valiyaveetil
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-10