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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue
Function
Amphipathic structure are what allows the interaction between hydrophobic properties of water, such as in the blood stream and hydrophobic lipids.
Apolipoprotein A-I is a protein APOA1 gene in humans that is a component of HDL, which a form of good cholesterol in human's diet, used in the transport of cholesterol and phospholipids in the body through the bloodstream in the reverse transport of cholesterol from the tissues to the liver of hepatocytes. They promote cholesterol efflux, a pathway in transferring intracellular cholesterol to extracellular acceptors, from tissues and act as a cofactor for the lecithin cholesterol acyltransferase (LCAT).
Disease
Clinical Significance
Structural highlights
Apolipoprotein a-1 (apoA-I) is a fairly small molecule that consists of a total of 243 residues and is 29-kD polypeptide in size. Structure in is shown in rainbow, in arrangement from N-terminus (red) of amine group to C-terminus (dark blue) end of carboxyl group.
Apolipoprotein a-1 in the monomer form truncated (lacking 1-43 residues) consists of unique pseudo-continuous alpha helix highlighted by kinks at , spaced approximately every 22 residues.
References
1. Voet, D., Voet, J. G., & Pratt, C. W. (2016). Fundamentals of Biochemistry (5th ed.). Hoboken, NJ: John Wiley & Sons.
- ↑ Voet, D., Voet, J. G., & Pratt, C. W. (2016). Fundamentals of Biochemistry (5th ed.). Hoboken, NJ: John Wiley & Sons.
2. APOA1 gene: MedlinePlus Genetics. (2020, August 18). Retrieved October 26, 2020, from https://medlineplus.gov/genetics/gene/apoa1/
3. Mangaraj, M., Nanda, R., & Panda, S. (2016, July). Apolipoprotein A-I: A Molecule of Diverse Function. Retrieved November 04, 2020, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4910842
