Date of Award


Degree Type


Degree Name

Master of Science in Natural Science


Chemistry and Biochemistry

First Advisor

Dr. Odutayo Odunuga

Second Advisor

Dr. Darrell Fry

Third Advisor

Dr. Michele Harris

Fourth Advisor

Dr. Josephine Taylor


Striated Muscle UNC-45, also known as UNC-45b, is an important protein that acts as a chaperone for myosin in cardiac and skeletal muscles, binding to myosin at its C-terminal UCS domain and regulating its assembly into thick filaments and sarcomeric structures. The UCS domain contains a large loop that is believed to be the first point of interaction between myosin and UNC-45b. GATA-4 is an essential transcription factor that facilitates transcription of several genes in cardiac development, particularly alpha-heavy chain myosin in heart tissue. Recently, studies have shown that there is interaction of GATA-4 with UNC-45b and that GATA-4 binds to the UCS domain. The implications of this interaction suggests that UNC-45b may play a role in not only the folding of myosin, but in the transcription of it as well. The aim of this study was to identify potential interaction interfaces between GATA-4 and the loop of UNC-45b and determine if the interactions are specific through computational models. Computational analysis suggests that the UCS loop is the preferential binding site of GATA-4 and that van der Waals packing is the primary method of binding.

Creative Commons License

Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.



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