Effects of Cardiac Arrhythmic Mutant D95V on Calmodulin Structure and Stability
Location
CSU Ballroom
Start Date
18-4-2016 10:00 AM
End Date
18-4-2016 11:30 AM
Student's Major
Chemistry and Geology
Student's College
Science, Engineering and Technology
Mentor's Name
Rebecca Moen
Mentor's Department
Chemistry and Geology
Mentor's College
Science, Engineering and Technology
Description
Calmodulin (CaM) is a small, highly conserved, ubiquitous calcium regulating protein. The structure consists of two lobes, an N-terminal lobe and a C-terminal lobe, each one binding two calcium ions for a total of four calcium ions per CaM molecule. CaM interacts with a vast number of proteins throughout the human body. CaM binds to calcium/calmodulin protein kinase II (CaMKII) in cardiac cells which regulates calcium homeostasis. There are five point mutations found in CaM that cause cardiac diseases such as arrhythmias. The physiological and diagnostic effects of the different CaM mutations have on humans have been studied in varying depth depending on the mutation. The specific mutation D95V on the second human CaM gene known as CALM2, was first discovered in infants with recurrent cardiac arrest. The mutation is located near a calcium binding site in the C-terminal lobe of CaM and therefore directly affects the binding affinity of calcium to CaM. The D95V point mutation was generated using site-directed mutagenesis and the mutated DNA was amplified using polymerase chain reaction (PCR). Recombinant protein technology was used to isolate the mutant CaM protein which was then purified using phenyl sepharose chromatography. The overall goal is determine changes in CaM structural dynamics and its interaction with CaMKII.
Effects of Cardiac Arrhythmic Mutant D95V on Calmodulin Structure and Stability
CSU Ballroom
Calmodulin (CaM) is a small, highly conserved, ubiquitous calcium regulating protein. The structure consists of two lobes, an N-terminal lobe and a C-terminal lobe, each one binding two calcium ions for a total of four calcium ions per CaM molecule. CaM interacts with a vast number of proteins throughout the human body. CaM binds to calcium/calmodulin protein kinase II (CaMKII) in cardiac cells which regulates calcium homeostasis. There are five point mutations found in CaM that cause cardiac diseases such as arrhythmias. The physiological and diagnostic effects of the different CaM mutations have on humans have been studied in varying depth depending on the mutation. The specific mutation D95V on the second human CaM gene known as CALM2, was first discovered in infants with recurrent cardiac arrest. The mutation is located near a calcium binding site in the C-terminal lobe of CaM and therefore directly affects the binding affinity of calcium to CaM. The D95V point mutation was generated using site-directed mutagenesis and the mutated DNA was amplified using polymerase chain reaction (PCR). Recombinant protein technology was used to isolate the mutant CaM protein which was then purified using phenyl sepharose chromatography. The overall goal is determine changes in CaM structural dynamics and its interaction with CaMKII.
Recommended Citation
Ranke, Jessica. "Effects of Cardiac Arrhythmic Mutant D95V on Calmodulin Structure and Stability." Undergraduate Research Symposium, Mankato, MN, April 18, 2016.
https://cornerstone.lib.mnsu.edu/urs/2016/poster-session-A/34
