Class

Article

College

College of Science

Department

Chemistry and Biochemistry Department

Faculty Mentor

Joan Hevel

Presentation Type

Poster Presentation

Abstract

PRMT is an enzyme that:

  • Methylates protein targets without use of a consensus sequence
  • Has implications in embryonic development, carcinogenesis, cardiac health and many other diseases1,2,3
  • Has 9 isoforms. Native PRMT1 is tetrameric (figure 1)

The mechanisms underlying PRMT target recognition and binding are unknown, limiting the study of PRMT related diseases. However: •

  • Proteomics have identified thousands of PRMT targets4
  • Commonalities in secondary structure may indicate a recognition element2
  • Prior research predicted (with JPred5) a surprising proportion (20.35%) of target methylation sites within alpha helices of proteins (figure 2).

Location

Logan, UT

Start Date

4-10-2024 10:30 AM

End Date

4-10-2024 11:20 AM

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Included in

Life Sciences Commons

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Apr 10th, 10:30 AM Apr 10th, 11:20 AM

Searching for Commonalities in Secondary Structure of PRMT Targets With Python Programming

Logan, UT

PRMT is an enzyme that:

  • Methylates protein targets without use of a consensus sequence
  • Has implications in embryonic development, carcinogenesis, cardiac health and many other diseases1,2,3
  • Has 9 isoforms. Native PRMT1 is tetrameric (figure 1)

The mechanisms underlying PRMT target recognition and binding are unknown, limiting the study of PRMT related diseases. However: •

  • Proteomics have identified thousands of PRMT targets4
  • Commonalities in secondary structure may indicate a recognition element2
  • Prior research predicted (with JPred5) a surprising proportion (20.35%) of target methylation sites within alpha helices of proteins (figure 2).