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The plant cell wall is strengthened by the molecular structure of cellulose. Cellulose is made up of ß-glucose arranged upside down, this arrangement aided hydrogen bonds between the hydrogen ions of the hydroxyl group and oxygen of the of the ring of same betta -glucose.
The aggregation of the hydrogen bonds give bundles of strong tensile strength of cellulose called the microfibrils (of 60-70 celluose molecules).They are held together in bundled called fibers.T<u>hese is the source of plant cell walls strength.
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Collagen is the main extracellur matrix (EM) in animal cells.It is a glycoprotein made up of 25%of body protein of animals.Each collagen molecule is made of helix shaped ,three polypeptide chains, wound around each other to form<u> triple helix.</u>The bonds holding helix together are hydrogen and covalent bonds.
Each triple helix is attached to adjacent collagen molecule, parallel to it. The covalent bonds formed a cross link which held the collagen molecules together forming FIBRILS. This gives flexibility to collagen, while maitaing strong tensile strength. This is what is responsible for the structural strength of cell membrane
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.The EM,is futher reinforced with carbohydrate molecules(proteoglycans) which<u> aided in water movements by osmosis following sodium movements into the matrix.</u>
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The answer is in the picture
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I don't really know how to explain I mean cells were just made that way so I hope this answer helped.
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Transcription is the process by which the information in a strand of DNA is copied into a new molecule of messenger
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One of the common genetic disorders is sickle cell anemia, in which 2 recessive alleles must meet to allow for destruction and alteration in the morphology of red blood cells. This usually leads to loss of proper binding of oxygen to hemoglobin and curved, sickle-shaped erythrocytes. The mutation causing this disease occurs in the 6th codon of the HBB gene encoding the hemoglobin subunit β (β-globin), a protein, serving as an integral part of the adult hemoglobin A (HbA), which is a heterotetramer of 2 α chains and 2 β chains that is responsible for binding to the oxygen in the blood. This mutation changes a charged glutamic acid to a hydrophobic valine residue and disrupts the tertiary structure and stability of the hemoglobin molecule. Since in the field of protein intrinsic disorder, charged and polar residues are typically considered as disorder promoting, in opposite to the order-promoting non-polar hydrophobic residues, in this study we attempted to answer a question if intrinsic disorder might have a role in the pathogenesis of sickle cell anemia. To this end, several disorder predictors were utilized to evaluate the presence of intrinsically disordered regions in all subunits of human hemoglobin: α, β, δ, ε, ζ, γ1, and γ2. Then, structural analysis was completed by using the SWISS-MODEL Repository to visualize the outputs of the disorder predictors. Finally, Uniprot STRING and D2P2 were used to determine biochemical interactome and protein partners for each hemoglobin subunit along with analyzing their posttranslational modifications. All these properties were used to determine any differences between the 6 different types of subunits of hemoglobin and to correlate the mutation leading to sickle cell anemia with intrinsic disorder propensity.
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