Folding of the disulfide containing protein, Ribonuclease A, using aromatic thiols

CHED 224

Lissette Perez, lpere018@fiu.edu, Yenia Silva, ysilv002@fiu.edu, Elvis J. Barrett, and Watson J. Lees, leeswj@fiu.edu. Department of Chemistry and Biochemistry, Florida International University, 11200 SW 8th Street CP 314, Miami, FL 33199
Protein folding processes are very complex, and essential for the proper functioning of organisms. If proteins fail to fold quickly and correctly, it is possible that insoluble aggregates, also known as inclusion bodies, will form. This in turn will make the protein inactive and unable to perform its normal activities. One of the problems with the traditional methods of protein folding is the fact that they are time consuming and low yielding. Ribonuclease A, RNase A, a protein that contains 4 disulfide bridges, is used as a model system to study the refolding of disulfide containing proteins in vitro. To improve the refolding of this protein to its native state, aromatic thiols containing ethylene glycol units will be used. These compounds can be utilized to improve the folding rate of other disulfide containing proteins.
 

Undergraduate Research Poster Session: Biochemistry
2:30 PM-4:30 PM, Monday, 11 September 2006 Moscone Center -- Hall D, Poster

Division of Chemical Education

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006