Start Date
2018
Description
In our lungs, there are lipids and lung proteins that work together to allow us to breathe. The proteins are known to encourage non-lamellar phases in lipids, but the function of this property for letting us to breathe is not well understood. The aim of my research was to qualify the behavior of the lipid MNd without any lung protein to allow for a comparison between the effects when formed naturally and when formed with lung protein to give a better understanding of what the protein is doing. Below is a diagram of an MNd molecule. In the presence of water, it forms various structures (or phases) because of its hydrophobic tail and hydrophilic head.
Recommended Citation
Kuiper, Daniel J. and Harper, Paul, "Structural parameters of MNd measured by X-ray diffraction" (2018). Summer Research. 18.
https://digitalcommons.calvin.edu/summer_research/2018/Posters/18
Included in
Structural parameters of MNd measured by X-ray diffraction
In our lungs, there are lipids and lung proteins that work together to allow us to breathe. The proteins are known to encourage non-lamellar phases in lipids, but the function of this property for letting us to breathe is not well understood. The aim of my research was to qualify the behavior of the lipid MNd without any lung protein to allow for a comparison between the effects when formed naturally and when formed with lung protein to give a better understanding of what the protein is doing. Below is a diagram of an MNd molecule. In the presence of water, it forms various structures (or phases) because of its hydrophobic tail and hydrophilic head.