How The Cells Are The Way Of Life?

823 WordsApr 3, 20174 Pages
Everyone should already know that cells are the way of life! But the real question is, what keeps those cells going? The cell has many different organelles such as the cell membrane, cell wall, chlorophyll, chloroplasts, cytoplasm, golgi apparatus, lysosomes, microtubules, mitochondria, nucleolus, nucleus, ribosomes, rough endoplasmic reticulum (rough ER), smooth endoplasmic reticulum (smooth ER), and the vacuole (Alberts, B. 2014). Out of all the organelles listed above, there are four that are involved with making up proteins-the nucleus, ribosomes, rough ER, and the golgi apparatus (Alberts, B. 2014). Proteins are very critical to cells, because they happen to be assembled by proteins, which in turn becomes major jobs that it does for…show more content…
2014). Ultimately, a protein can take on the tertiary structure which is a combination of all the secondary structures (Alberts, B. 2014). Furthermore, most proteins take on the quaternary structure which consist of two or more polypeptide chains that form a protein complex of a honomer or heteromer (Alberts, B. 2014). The selective protein that will be discussed is ferredoxin- NADP reductase. Ferredoxin provides regulation by diminishing substitutes between ferredoxin and NADP in the photosynthetic electron transport chains of the Calvin Cycle in the individual cell and organism that it is present in (Alcantara-Sanchez, F., L. Leyva-Castillo, A. Chagolla-Lopez, L. Gonzalez de la Vara, and C. Gomez-Lojero. 2017). Ferredoxin NADP reductase is structural and an enzyme. It is not in all organism and cells. However, it is in the organisms of plants, bacteria and in the eukaryotes mitochondria (Ferredoxin—NADP( ) reductase. 2017). The structure for ferredoxin NADP reductase has been determined in the Protein Data Bank. It has a variety of information available about ferredoxin NADP reductase. Information from the structure summary and the 3D view ferredoxin NADP reductase has the primary structure, which consists of its amino acid sequence, shown in figure 2 (Shinohara, F., G. Kurisu, G. Hanke, C. Bowsher, T. Hase, and Y. Kimata-Ariga). It has a secondary
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