Event Title

Studying the Structure and Stability of F141L Calmodulin Mutant in the Assessment of Cardiac Related Complications

Location

CSU Ballroom

Start Date

18-4-2016 10:00 AM

End Date

18-4-2016 11:00 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 ubiquitous protein that carries many different important roles within eukaryotes organisms. Its most recognized role is its ability to efficiently sense and bind calcium (Ca2+) when there is an influx within the intracellular compartments of cells. By binding Ca2+, CaM is able to interact and signal many other proteins in a very quick manner. Being that it is such a nimble protein, it has great importance in the cells of cardiac and skeletal muscle. Within these spaces CaM binds Ca2+ and signals calmodulin-dependent protein kinase II (CaMKII), which then goes on to phosphorylate ryanodine receptor 2, thus controlling the Ca2+ flux. When the genes that code for CaM become mutated, many dangerous disease states manifest. Focusing on one mutant variant specifically, F141L, is phenotypically expressed by recurrent cardiac arrest (RCA) and early onset severe long QT (EsLQT). This being only one of many fatal cardiac related diseases arising from mutated CaM, there is much work going into the underpinnings of the biochemical and biophysical implications of such mutants. This study aims to further this understanding by creating mutated CaM protein by use of recombinant protein expression technology, then studying its structural dynamics. The assays that will be utilized will aim to look at the stability and structure of the F141L mutant. The stability test will be carried out by thermal denaturation and the structure by circular dichroism. Gaining a better understanding of these aspects will help in the production of possible pharmaceuticals targeting CaM related issues.

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Apr 18th, 10:00 AM Apr 18th, 11:00 AM

Studying the Structure and Stability of F141L Calmodulin Mutant in the Assessment of Cardiac Related Complications

CSU Ballroom

Calmodulin (CaM) is a ubiquitous protein that carries many different important roles within eukaryotes organisms. Its most recognized role is its ability to efficiently sense and bind calcium (Ca2+) when there is an influx within the intracellular compartments of cells. By binding Ca2+, CaM is able to interact and signal many other proteins in a very quick manner. Being that it is such a nimble protein, it has great importance in the cells of cardiac and skeletal muscle. Within these spaces CaM binds Ca2+ and signals calmodulin-dependent protein kinase II (CaMKII), which then goes on to phosphorylate ryanodine receptor 2, thus controlling the Ca2+ flux. When the genes that code for CaM become mutated, many dangerous disease states manifest. Focusing on one mutant variant specifically, F141L, is phenotypically expressed by recurrent cardiac arrest (RCA) and early onset severe long QT (EsLQT). This being only one of many fatal cardiac related diseases arising from mutated CaM, there is much work going into the underpinnings of the biochemical and biophysical implications of such mutants. This study aims to further this understanding by creating mutated CaM protein by use of recombinant protein expression technology, then studying its structural dynamics. The assays that will be utilized will aim to look at the stability and structure of the F141L mutant. The stability test will be carried out by thermal denaturation and the structure by circular dichroism. Gaining a better understanding of these aspects will help in the production of possible pharmaceuticals targeting CaM related issues.

Recommended Citation

Kampmeyer, Drew. "Studying the Structure and Stability of F141L Calmodulin Mutant in the Assessment of Cardiac Related Complications." Undergraduate Research Symposium, Mankato, MN, April 18, 2016.
http://cornerstone.lib.mnsu.edu/urs/2016/poster-session-A/40