News From Terre Haute, Indiana

Schools

August 15, 2012

ISU’s Facebook app helps acquaint students

TERRE HAUTE — After Brooklyn Hollis received her acceptance letter to Indiana State University, she decided to visit the university’s new Facebook application to learn more.

She now spends more time there than on her own Facebook page.

Hollis has met friends and classmates, posed questions and answered others and learned more about ISU through the university’s application on the social media website. The app, which Indiana State social media developer Amy Bouman described as a “Facebook within a Facebook for ISU students,” includes message boards for students to talk and pose questions to each other or to Indiana State admissions officers who also use the application.

“I’ve actually met my best friends through that site,” said Hollis, an incoming first-year student from Crawfordsviile. “That was the most exciting thing, meeting girls my age who are going through the same thing I am, moving away from home.”

Indiana State initially offered the application to incoming first-year students in the Class of 2016. Students using the app can create plans to meet up, promote their events, form study groups and join communities that interest them, which can be based on their major, interests or activities that they want to be involved in on campus, Bouman said.

More than 1,500 incoming first-year students have already registered for the app, and they have posted 22,424 times, engaged in 3,843 conversations and created 4,018 communities so far.

“It’s a private community, so only other ISU students see their posts,” Bouman added. “The idea is to get them to meet other students that they might not have met.”

Flurkey said researchers hoped to understand more about the enzyme but real-world  applications of the research are still in the distant future.

The first study was to protect the latent form of the mushroom tyrosinase by adding protease inhibitors.  

“We are trying to determine if there is a way to preserve the latent form,” Flurkey said. “If we can do that, we can do studies on the dormant form.”

The second study looked at activating the enzyme by using a detergent and then removing that detergent to see if it is possible to return it back to its latent form.

“It’s been proposed that once you activate it, it stays active but we are seeing if it is reversible,” Lutjemeyer said.

He said they were able to convert some back to latent but less than expected.

The third study focused on the separation of active and latent forms of tyrosinase using chromatography methods.

“Usually biochemists like to study different forms of enzymes,” Flurkey said. “So it would be nice to be able to separate them so you can study them individually.”

 

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