Investigation of molecular condensation on air-liquid interface for protein crystallization

S. Takasawa, S. Hosoda, Y. Yamanishi

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

This paper investigated the mechanism of the condensation of protein molecules on air-liquid interface of bubbles. Electrically charged bubbles were confirmed to have clear advantage of producing protein crystal over general bubbles or conventional vapor diffusion method for the first time. The adsorption force between the protein molecular and air-liquid interface of bubble was successfully measured using force sensing optical tweezers. These findings contribute to the effective production of protein crystal and to the protein crystallography.

Original languageEnglish
Title of host publication2015 Transducers - 2015 18th International Conference on Solid-State Sensors, Actuators and Microsystems, TRANSDUCERS 2015
PublisherInstitute of Electrical and Electronics Engineers Inc.
Pages440-443
Number of pages4
ISBN (Print)9781479989553
DOIs
Publication statusPublished - 2015 Aug 5
Event18th International Conference on Solid-State Sensors, Actuators and Microsystems, TRANSDUCERS 2015 - Anchorage, United States
Duration: 2015 Jun 212015 Jun 25

Other

Other18th International Conference on Solid-State Sensors, Actuators and Microsystems, TRANSDUCERS 2015
CountryUnited States
CityAnchorage
Period15/6/2115/6/25

Keywords

  • Air-liquid Interface and Protein Crystal
  • Micro-bubble
  • Optical Tweezer

ASJC Scopus subject areas

  • Instrumentation
  • Electrical and Electronic Engineering

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  • Cite this

    Takasawa, S., Hosoda, S., & Yamanishi, Y. (2015). Investigation of molecular condensation on air-liquid interface for protein crystallization. In 2015 Transducers - 2015 18th International Conference on Solid-State Sensors, Actuators and Microsystems, TRANSDUCERS 2015 (pp. 440-443). [7180955] Institute of Electrical and Electronics Engineers Inc.. https://doi.org/10.1109/TRANSDUCERS.2015.7180955