Location

Stephen F Austin State University, Baker Pattillo Student Center, Regent's Suite A and Twilight Ballroom

Start Date

7-4-2011 4:00 PM

End Date

7-4-2011 8:00 PM

Description

UNC-45 is an important protein for muscle contraction and heart formation. The UNC-45 protein is a chaperone for the myosin heavy chain head, and UNC-45 only binds to the UCS domain of the myosin head. In our research for the interaction of myosin and UNC-45. The mutation was accomplished using the multiple sequence alignment method and site-directed mutagenesis. The mutations were generated in UNC-45 of Mus musculus (mouse), and the specific amino acids that were mutated were: L741A and L860F. The mutant proteins were sequenced and over-expressed for analysis.

Included in

Biochemistry Commons

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Apr 7th, 4:00 PM Apr 7th, 8:00 PM

Analysis of Critical Amino Acid Residues in UNC-45 necessary for its Interaction with Myosin Using Site-Directed Mutagenesis

Stephen F Austin State University, Baker Pattillo Student Center, Regent's Suite A and Twilight Ballroom

UNC-45 is an important protein for muscle contraction and heart formation. The UNC-45 protein is a chaperone for the myosin heavy chain head, and UNC-45 only binds to the UCS domain of the myosin head. In our research for the interaction of myosin and UNC-45. The mutation was accomplished using the multiple sequence alignment method and site-directed mutagenesis. The mutations were generated in UNC-45 of Mus musculus (mouse), and the specific amino acids that were mutated were: L741A and L860F. The mutant proteins were sequenced and over-expressed for analysis.