Jan Peter Birkner
University of Groningen
6 Papers
30 Citations
Jan Peter Birkner is an academic researcher from University of Groningen. The author has contributed to research in topics: Mechanosensitive channels & Gating. The author has an hindex of 5, co-authored 6 publications.
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Papers
Bacillus subtilis spore protein SpoVAC functions as a mechanosensitive channel
TL;DR: The data indicate that SpoVAC acts as a mechanosensitive channel and has properties that would allow the release of Ca‐DPA and amino acids during germination of the spore.
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The activation mode of the mechanosensitive ion channel, MscL, by lysophosphatidylcholine differs from tension-induced gating
Nobina Mukherjee,Mac Donald F. Jose,Jan Peter Birkner,Martin Walko,Helgi I. Ingólfsson,Anna Dimitrova,Clement Arnarez,Siewert J. Marrink,Armagan Kocer +8 more
TL;DR: The activation mode of the mechanosensitive ion channel, MscL, by lysophosphatidylcholine differs from tension‐induced gating, leading to the conclusion that the mode of action of LPC is different from that of applied tension.
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On the role of individual subunits in MscL gating: "all for one, one for all?".
TL;DR: A chemically addressable heteropentameric MscL is created, which allows us to selectively trigger only one subunit in the pentameric protein assembly, and it is shown that a decrease in the hydrophobicity of a pore residue in only oneSubunit breaks the energy barrier for gating and increases the pore diameter up to 10 Å.
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Studying mechanosensitive ion channels with an automated patch clamp.
Maria Barthmes,Mac Donald F. Jose,Jan Peter Birkner,Andrea Brüggemann,Christian Wahl-Schott,Armagan Kocer +5 more
TL;DR: Activation and single channel analysis of a bacterial mechanosensitive ion channel using an automated patch clamp system and the tension sensitivity and channel kinetics data obtained were in good agreement with that obtained from the conventional patch clamp.
8
Hydrophobic gating of mechanosensitive channel of large conductance evidenced by single-subunit resolution
TL;DR: This work gradually changed the hydrophobicity of the pore constriction in this homopentameric protein by modifying a critical pore residue one subunit at a time, which allows single-subunit resolution for manipulating and monitoring “mechanosensitive channel of large conductance” from Escherichia coli.