Measurement of protein hydration shells using a quartz microbalance

L. Reinisch, R. D. Kaiser, and J. Krim
Phys. Rev. Lett. 63, 1743 – Published 16 October 1989
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Abstract

The protein myoglobin is dried on the surface electrodes of a 5-MHz quartz crystal oscillator. As the humidity above the film increases, the protein absorbs water and develops a hydration shell. The oscillator frequency shift measures the mass of absorbed water. Incremental decreases in the amplitude of vibration are also observed, corresponding to a softening of the protein structure and subsequent energy dissipation (damping) of the oscillations. The transition of a protein from a dry, more rigid structure to a semifluid hydrated state is observed to occur in discrete steps.

  • Received 6 March 1989

DOI:https://doi.org/10.1103/PhysRevLett.63.1743

©1989 American Physical Society

Authors & Affiliations

L. Reinisch

  • Department of Radiology and the Laser Biophysics Center, Uniformed Services University, 4301 Jones Bridge Road, Bethesda, Maryland 20814

R. D. Kaiser and J. Krim

  • Department of Physics, Northeastern University, 360 Huntington Avenue, Boston Massachusetts 02115

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Vol. 63, Iss. 16 — 16 October 1989

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