What is amylose? Amylose synthesis itself is simple, and is the linear chains formed through processive elongation by  a single enzyme, the Granule Bound Starch Synthase ( GBSS). GBSS is the glucosyltransferase responsible for elongating polymers and was the only protein known to be required for it’s biosynthesis. The Protein Targeting to Starch (PTST) is also specifically required for amylose synthesis in Arabidopsis. PTST is a plastidial protein possessing an N-  terminal coiled coil domain, and a C- terminal carbohydrate binding module (CBM). It was discovered that ARABIDOPSIS PTST mutants synthesize amylose-free starch  and are phenotypically similar to mutants lacking (GBSS). Mutation of the CBM of PTST caused GBSS to remain in the plastic stroma. PTST fulfills an unknown function in targeting GBSS in starch. This sheds new light on the importance of targeting bio-synthetic enzymes to sub-cellular sites where their action is required. PTST is promising a new gene target for the biotechnological modification of starch compositions as it is exclusively involved in amylose synthesis. GBSS protein which normally binds to starch cannot bind in the absence of PTST. This discovery sheds new light on a previously unknown protein targeting process where enzymes are delivered to the starch.

There are lots of proteins in a single cell. They come in every size and shape and type and each one has a unique and specific job. Some are structural parts, giving cells shape or helping them move. Others act as signals drifting between cells like messages in a bottle. Others are metabolic enzymes putting together or snapping apart bio-molecules needed by the cell. Proteins are the most abundant organic molecules in living systems and are way more diverse in structure and function than other classes of macro-molecules. A single cell can contain a thousand proteins each with a unique function, although their structures like their functions vary greatly. All proteins are made up of one or more chains of amino acid. We will look at the building blocks and the structures and roles of proteins. One example of a enzyme found in your body is salivary amylase which breaks amylose (a kind of starch ) down into smaller sugar. The amylose is not sweet tasting but the smaller sugar tastes sweet. This is why starchy foods often taste sweet. Chew chew chew, gives them longer times for salivary amylase to get to work.

Hormones are chemical signals released by the endocrine cells like the cells of your pituitary gland. They control physiological processes such as growth development, development metabolism and reproduction. While some hormones are steroid based others are proteins. These are called peptide hormones. Insulin binds to cells in the liver and other parts of the body causing them parts of the body causing them to take up the glucose. This process helps return the blood sugar to its normal resting levels.

Some proteins are the Digestive enzyme, transparent, structure, Hormone signalling, Defence.  Amino acids are the monomers that made up the proteins. A protein us made up of one or more linear chains of amino acids each of which is called a poly – peptide. Amino group can be protonated  and bears a positive or negative charge.

Antigens are markers that tell the body your body that something is foreign. Your immune cells make antibodies to recognize and destroy harmful antigens in fact think of antigens as antibody generators. They destroy any foreign in your body. Proteins caused in response to antigens. Antibodies are protective proteins produced by your immune system. They attract antigens foreign substances such as bacteria, fungi, viruses, and toxins. and remove them from your body. Antigens play a crucial role in body immunity and play a crucial role in the prevention and elimination of disease. Antigens can be proteins, peptide, amino acid chains  polysaccharide (chains of simple sugar) lipids or nucleic acids. Antigens insist on normal cells.

Nuclear lipids play a role in the proliferation, differentiation, and apoptic process. Cellular nuclei contain high levels of phosphatidylcholine and sphingomyelin which are partially linked to cholesterol and proteins to form lipid proteins complexes. Different mixtures of lipids are found in the membrane of cells of different types as well as in the various membranes of a single eukaryotic cell.  The head groups of some lipids form docking sites for specific cytosolic proteins. They can act as building blocks for cellular structures.

Those nucleic lipids can act as building blocks for specific cytosolic or cytosine type proteins in building cellular structures . So you know those folded proteins that they are finding in veins as embalmers can they take a look at those proteins mutated? If a virus attacks our immune system, and enters the Ace 2, there is no reason why this attack would not upset the homeostasis of the Immunoglobulin processes, and that is related to the helix and our DNA. Cytosine being an amino acid.

If partial IFN -yR2 deficiency is due to protein misfolding and can be rescued by inhibitors of glycosylation-PMC. Failure of protein QC systems to manage protein loads can result in protein aggregation and or formation of of toxic protein species. The accumulation of misfolded proteins is the hallmark of a number of new diseases, including neuro degeneration, cardiovascular diseases, cataract and age related macular degeneration. A protein is considered mutated if it cannot achieve it’s normal native state.

 

Carolyn d Hogarth Canada

Thank you for reading my post….