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The following chart shows the solubility of various ionic compounds in water at 1 atm pressure and room temperature (approx. 25 °C, 298.15 K). "Soluble" means the ionic compound doesn't precipitate, while "slightly soluble" and "insoluble" mean that a solid will precipitate; "slightly soluble" compounds like calcium sulfate may require heat to precipitate.
The tables below provides information on the variation of solubility of different substances (mostly inorganic compounds) in water with temperature, at one atmosphere pressure. Units of solubility are given in grams of substance per 100 millilitres of water (g/100 ml), unless shown otherwise. The substances are listed in alphabetical order.
The result: 1 liter of water can dissolve 1.34 × 10 −5 moles of AgCl at room temperature. Compared with other salts, AgCl is poorly soluble in water. For instance, table salt (NaCl) has a much higher K sp = 36 and is, therefore, more soluble. The following table gives an overview of solubility rules for various ionic compounds.
Organotrophs use organic compounds as electron/hydrogen donors. Lithotrophs use inorganic compounds as electron/hydrogen donors.. The electrons or hydrogen atoms from reducing equivalents (electron donors) are needed by both phototrophs and chemotrophs in reduction-oxidation reactions that transfer energy in the anabolic processes of ATP synthesis (in heterotrophs) or biosynthesis (in autotrophs).
In protein synthesis (such as Fmoc solid-state synthesizers), the N-terminus is often used as the attachment site on which the amino acid monomers are added. To enhance the electrophilicity of carboxylate group, the negatively charged oxygen must first be "activated" into a better leaving group. DCC is used for this purpose.
In organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another.
Usually, it is located on the outer surface of the protein, making it water-soluble. It binds to positively charged molecules and ions, and is often used in enzymes to fix the metal ion. When located inside of the protein, aspartate and glutamate are usually paired with arginine and lysine. Glutamic acid: E Glu
The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s). [2] The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate - GlcA - Gal -Gal- Xyl -PROTEIN).