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Kansas State University
128 Dole Hall
Manhattan, KS 66506
785-532-2535
media@k-state.edu
Information provided by K-State News Services may be reproduced without permission. The marks and names of Kansas State University are protected trademarks and may not be used in any commercial or private endeavor without the approval of the university.

Biotechnology Core Facility

Director: John M. Tomich
Address: Burt Hall, rooms 201, 207 and 216
Phone number: 785-532-5956
Website: http://www.k-state.edu/bchem/biotech/

 

The Biotechnology Core Facility at Kansas State University was established in 1993 to provide a number of centralized services to plant and animal researchers at K-State and elsewhere. The goods and services provided by the facility give researchers the tools they need to identify new proteins, protein modifications, protein-protein interactions and enzyme substrates. The lab is located in space provided by the department of biochemistry and the facility is supported in part by fees for service and the K-State Colleges of Agriculture and Arts and Sciences.

The laboratory functions in three distinct ways: synthesis, separations and bioanalysis. The lab synthesizes peptides, peptide libraries, chromophores, fluorophores and other organic molecules. It also serves as a broker for ordering oligonucleotides. Separations are performed using various chromatographic techniques and by mass spectrometry. Bioanalysis is performed to assess purity, size, composition and sequences of peptides, proteins and carbohydrates. The facility is equipped with more than $1.75 million worth of automated scientific instruments that enhance the biotechnology capabilities of the university.

One piece of equipment, the Biacore, gives the core facility a new dimension, the quantification of molecular interactions. This instrument uses a treated gold slide that allows the covalent attachment and display of molecules, such as proteins or lipids, in a flow cell. Potential binding partners can be introduced in solution and subsequent binding to the bound molecule can be measured. Using this technique, accurate association constants can be determined.