Hailey R. Bureau, Ph.D

Registered Patent Agent

1-703-205 8038
Hailey Bureau

Hailey Bureau, Ph.D., specializes in patent prosecution in the fields of chemistry and life sciences. Her graduate work focused on developing algorithms for the simulation of peptide dynamics. Dr. Bureau received her B.S. in chemistry from the University of Tennessee-Knoxville and her Ph.D. in chemistry from the Georgia Institute of Technology. She is currently attending law school at the George Washington University.

Services

Speaking Engagements

    Current Speaking Engagements

  • Sep
    30

    BSKB to present at FICPI’s “Connect, Share & Grow” series

    FICPI’s “Connect, Share & Grow” Webinar Series.

    Webinar
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    Previous Speaking Engagements

  • A Joint Event Hosted By BSKB And World IP Review

    WIPR Influential Women in IP

    September 24 2019

Articles

  • April 28, 2020

    Indefinite claims at the PTAB

    by Chad M. Rink and Hailey R. Bureau, Ph.D. | World Intellectual Property Review

    Chad Rink and Hailey Bureau, Ph.D. talk about indefinite claims at the PTAB and alternative routes in WIPR- Issue 1.

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  • February 12, 2020

    The relative stability of trpzip1 and its mutants determined by computation and experiment

    by Hailey R. Bureau, Stephen Quirk and Rigoberto Hernandez | RSC Advances

    Six mutants of the tryptophan zipper peptide trpzip1 have been computationally and experimentally characterized. We determine the varying roles in secondary structure stability of specific residues through a mutation assay. Four of the mutations directly effect the Trp–Trp interactions and two of the mutations target the salt bridge between Glu5 and Lys8. CD spectra and thermal unfolding are used to determine the secondary structure and stability of the mutants compared to the wildtype peptide. Adaptive steered molecular dynamics has been used to obtain the energetics of the unfolding pathways of the mutations. The hydrogen bonding patterns and side-chain interactions over the course of unfolding have also been calculated and compared to wildtype trpzip1. The key finding from this work is the importance of a stabilizing non-native salt bridge pair present in the K8L mutation.

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Presentations