Additional Funding Sources
This project was supported by the National Science Foundation under Grant No. 1554166.
Abstract
Artificial membrane systems are often used as model membranes for the reconstitution of protein channels and the investigation of their transport properties. However, a correct interpretation of their biophysical properties requires an extensive analysis of electrophysiology data recorded with the instrument. While the recording programs provide a raw analysis of the experimental data and a preliminary plot, they lack a complete description in terms of input and output parameters, and a statistical analysis is missing. To expedite the analysis process, we used the R program to completely analyze raw data provided by the ClampFit software package for measuring the selectivity of the protein channel lysenin. Besides providing a reliable analysis of experimental data, the program may be expanded to include other necessary assessments ranging from investigating membrane integrity to determining the open probability and free energies characteristic to conformational changes of channels.
Using R to Analyze Data on the Electrical Properties of Membranes
Artificial membrane systems are often used as model membranes for the reconstitution of protein channels and the investigation of their transport properties. However, a correct interpretation of their biophysical properties requires an extensive analysis of electrophysiology data recorded with the instrument. While the recording programs provide a raw analysis of the experimental data and a preliminary plot, they lack a complete description in terms of input and output parameters, and a statistical analysis is missing. To expedite the analysis process, we used the R program to completely analyze raw data provided by the ClampFit software package for measuring the selectivity of the protein channel lysenin. Besides providing a reliable analysis of experimental data, the program may be expanded to include other necessary assessments ranging from investigating membrane integrity to determining the open probability and free energies characteristic to conformational changes of channels.