By G. Waite, L. Waite
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Extra info for Applied Cell and Molecular Biology for Engineers
4 Chapter One Proteins As can be noted from the structure of the R groups of the amino acids, many contain substituents that are either fully ionized at physiological pH (aspartate and lysine for example) or possess partial charges and are thus polar, such as the tyrosyl hydroxyl. The consequence of these facts are that fully ionized R group substituents such as ϪNH3ϩ and ϪCOOϪ can form intramolecular electrostatic bonds and cause polypeptide chains to fold back on themselves. Similarly, R groups that are distant from each other in the polymer chain and that are capable of forming hydrogen bonds can interact intramolecularly, further stabilizing the folded three-dimensional conformer of a protein.
20, are generally referred to as liposomes while particles of ambiguous shape and form are generally referred to as vesicles. The key attributes of liposomes or vesicles are that they are formed of spherically closed bilayer membranes, with the hydrophobic acyl chains of phospholipids from the two sides of the membrane oriented to the inside of the bilayer and the polar portion of the phospholipids oriented toward the aqueous/polar environments on the exterior and interior of the nanoparticles.
These molecules are classed together mainly as a consequence of the fact that they contain moderately long stretches of mostly saturated, covalently bonded carbon atoms, are relatively insoluble in water, and are generally soluble in organic solvents. There are two main biological functions of this class of molecules. First, saturated hydrocarbon chains, mainly the fats, represent the principal and most chemically efficient storage form of biological energy. Second, a special class of lipids, known as phospholipids, are principal players in forming the hydrophobic barrier of cell membranes which separate the aqueous extracellular milieu from the mainly water-soluble material that comprises the cytosol or intracellular compartment of cells.
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