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Watching single protons bind

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Using single-molecule biophysical studies in an ion channel, the protonation state of engineered basic amino acids was measured in real time, making it possible to calculate the pKas of the substituted residues and creating a unique, comprehensive dataset for theorists studying the effects of an electrostatic environment on integral membrane protein function.

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Figure 1: Structure of the acetylcholine receptor channel used to measure the protonation state in real time of ionizable amino acids engineered into its channel-lining M2 segment.

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  1. the Departments of Physiology and Biophysics, Neuroscience and Medicine of the Albert Einstein College of Medicine of Yeshiva University, 1300 Morris Park Avenue, Bronx, 10461, New York, USA

    Myles H Akabas

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  1. Myles H Akabas
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Akabas, M. Watching single protons bind. Nat Chem Biol 2, 128–130 (2006). https://doi.org/10.1038/nchembio0306-128

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