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Preserving the Sequence of a Biopolymer’s Monomers as They Enter an Electrospray Mass Spectrometer

William Maulbetsch, Benjamin Wiener, William Poole, Joseph Bush, and Derek Stein
Phys. Rev. Applied 6, 054006 – Published 17 November 2016
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Abstract

This paper investigates how faithfully an electrospray mass spectrometer reports the order of monomers of a single biopolymer in the context of two sequencing strategies. We develop a simplified one-dimensional theoretical model of the dynamics of Brownian particles in the Taylor cone of an electropray source, where free monomers drift towards the apex in an elongational force gradient. The likelihood that neighboring particles will invert their order decreases near the apex because the strength of the force gradient increases. Neighboring monomers on a stretched biopolymer should be cleaved by photofragmentation within about 3 nm of the apex if they are to enter the mass spectrometer in sequence with 95% probability under typical experimental conditions. Alternatively, if the monomers are cleaved processively at milliseconds-long intervals by an enzyme, their sequence will be faithfully reported with 95% confidence if the enzyme is within about 117 nm of the apex.

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  • Received 1 September 2015

DOI:https://doi.org/10.1103/PhysRevApplied.6.054006

© 2016 American Physical Society

Physics Subject Headings (PhySH)

Physics of Living SystemsFluid DynamicsStatistical Physics & ThermodynamicsPolymers & Soft Matter

Synopsis

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Maintaining the Sequence

Published 17 November 2016

Theoretical calculations indicate that an electrospray-based technique could correctly read out the amino acid sequence of protein molecules.

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Authors & Affiliations

William Maulbetsch, Benjamin Wiener, William Poole, Joseph Bush, and Derek Stein

  • Physics Department, Brown University, Providence, Rhode Island 02912, USA

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Vol. 6, Iss. 5 — November 2016

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