Research Symposium

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The 21st annual Westmont College Spring Student Research Symposium

One of the hallmarks of Westmont College's academic program is the opportunity for undergraduate students to work directly with faculty on research projects. Work presented at the annual Spring Student Research Symposium includes student research conducted during the past year from all three divisions of the college (Humanities, Social Sciences, and the Natural and Behavioral Sciences). The purpose of this symposium is to celebrate the noteworthy accomplishments of Westmont students.

Wednesday, April 19th, 2017 3:30-5:30PM in Winter Hall Atrium

Refreshments will be served.

Research Symposium Details

Who should apply?

Any student in any major who has or is participating in a semester-long or longer research project under the supervision of a faculty member during this academic year can apply. This would include, but is not limited to, major honors students, independent research students, and students in a class with a significant cumulative research project (e.g. some senior capstone classes). Students working in partnership on the same project should apply together.

Symposium format

Each presenter or team prepares an overview of their research project in the form of a poster (max size: 48" x 36"). All posters are displayed throughout the 2-hour event and presenters stand by their poster to discuss the research with visitors and answer questions. Refreshments are available and visitors come and go at their convenience throughout the duration of the symposium.

Poster design and printing

Posters are usually made as one large “slide” in PowerPoint or Keynote, or in another graphics program. Printing can be done either locally and picked up or online and shipped here. Some options are below:

  • www.makesigns.com (also has templates you can download into PowerPoint; ships from Chicago)
  • The Print Center in Office Max (can be shipped to you or picked up at the store but maximum width for in store, same or next day pick-up is 24”)
  • Westmont Reprographics (may have limited availability and would need a minimum of 3 days lead time; 24” max width)

How to apply

Email your project title, list of authors (include the year of graduation and email address for each author), name of your faculty mentor (include their department), and a 150-word maximum abstract to Heidi Henes-Van Bergen at hhenesva@westmont.edu. Also, since sometimes student authors have graduated, are abroad, or are otherwise unavailable for the symposium, please underline the name(s) of the student(s) who will be presenting the poster. Please have all this either embedded in the email or attached separately as a Word document. Use the sample for guidance of how it should be formatted. Finally, if you have any special needs (e.g. a small table to display something or you need to be near an outlet, etc.) then include this as a note in your email.

Please submit your abstract to Heidi Henes-Van Bergen at hhenesva@westmont.edu.

DEADLINE IS MONDAY, APRIL 10th by 5PM.

Sample title/author list/abstract

The Role of TDP-43 Oligomerization of ALS Neurodegeneration

Brady Quon (’16) and Megan Korff (’16), Faculty Mentor: Kristi Cantrell, Chemistry

Author Email(s): author1@westmont.edu, author2@westmont.edu

Abstract : TAR-DNA-binding protein (TDP-43) is an RNA processing protein that is primarily located in the nucleus. Recent research supports that TDP-43 aggregation into fibrils and oligomers, as well as translocation into the cytoplasm, are characteristic of the neurodegenerative disease Amyotrophic Lateral Sclerosis (ALS). Several ALS-associated mutations have been found in the carboxyl terminal, glycine rich region of TDP-43. Six, 13 residue peptide fragments are currently being synthesized to elucidate the conformation and aggregation of the TDP-43 glycine-rich region. Fibril assays have been prepared from two of the purified peptides and imaged using electron microscopy. Thioflavin T was applied to any fibrillar aggregates to determine the presence of beta-sheet secondary structure.