Investigation of the biologically active forms of ZmHsp17.0-CII and ZmHsp17.6-CII

CHED 870

Tamutenda C. Chidawanyika, tchidawanyika08@wooster.edu1, Virginia B. Pett1, and Robert A. Bouchard2. (1) Department of Chemistry, The College of Wooster, 943 College Mall, Wooster, OH 44691, (2) Department of Horticulture and Crop Science, Ohio Agricultural Research & Development Center, 1680 Madison, Wooster, OH 44691
Small heat shock proteins (sHsps) are low molecular mass proteins (15 to 42 kDa) that can form oligomers of 200-800 kDa. The primary structure of sHsps includes the conserved α-crystallin domain. This domain is a major constituent of the human eye lens; mutations in this domain cause cataracts in the human eye. During times of stress caused by elevated temperatures, the presence of chemicals or heavy metals, changes in pH, and osmotic changes, sHsps are expressed and can function as molecular chaperones to prevent the aggregation and misfolding of other proteins in the cell. The purpose of this study was to learn more about the biologically active forms of Zea mays sHsps (ZmHsp17.0-CII, and ZmHsp17.6-CII) by determining how many protein subunits constitute the oligomer at various temperatures. Techniques used were native polyacrylamide gel electrophoresis (native PAGE) and blue native polyacrylamide gel electrophoresis (BN-PAGE).
 

Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, April 7, 2008 Morial Convention Center -- Hall A, Poster

Division of Chemical Education

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008