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| One of several organic compounds with the same molecular formula but different structures and therefore different properties. |
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| A specific configuration of atoms commonly attached to the carbon skeletons of organic molecules and usually involved in chemical reactions. |
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| An organic compound containing hydroxyl groups. |
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| An organic compound with a carbonyl group of which the carbon atom is bonded to two other carbons. |
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| An organic molecule with a carbonyl group located at the end of the carbon skeleton. |
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| A long molecule consisting of many similar or identical smaller molecules linked together. |
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| The sub-unit that serves as the building block of a larger molecule. |
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| A reaction in which two molecules become covalently bonded to each other through the loss of a small molecule, usually water; also called dehydration reaction. |
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| A chemical process that lyses, or splits, molecules by the addition of water; an essential process in digestion. |
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| One of a family of compounds, including fats, phospholipids, and steroids, that are insoluble in water. |
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| Three-dimensional biological polymers constructed from a set of 20 different monomers, called amino acids. |
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| Polymers (polynucleotides) consisting of many nucleotide monomers; serves as a blueprint foor proteins and, though the actions of proteins, for all cellular activities. The two types are DNA and RNA. |
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| A fatty acid in which all carbons in the hydrocarbon tail are connected by single bonds, thus maximizing the number of hydrogen atoms that can attach to the carbon skeleton. |
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| A fatty acid in which some carbons in the hydrocarbon tail are connected by double bonds, thus minimizing the number of hydrogen atoms that can attach to the carbon skeleton. |
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| The covalent bond between two amino acid units, formed by a dehydration reaction. |
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| Primary Structure of a Protein |
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| The level of protein structure referring to the specific sequence of amino acids. |
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| Secondary Structure of a Protein |
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| The localized, repetitive coiling or folding of the polypeptide backbone of a protein due to hydrogen bond formation between peptide linkages. |
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| Tertiary Structure of a Protein |
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| Irregular contortions of a protein molecule due to interactions of side chains involved in hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges. |
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| Quaternary Structure of a Protein |
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| The particular shape of a complex, aggregate protein, defined by the characteristic three-dimensional arrangement of its consistent subunits, each a polypeptide. |
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| Strong covalent bonds formed when the sulfur of one cysteine monomer bonds to the sulfur of another cysteine monomer. |
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| For proteins, a process in which a protein unravels and loses its native conformaaion, thereby becoming biologically inactive. For DNA, the separation of the two strands of the double helix. This occurs under extreme conditions of pH, salt concentration, and temperature. |
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| A double-stranded, helical nucleic acid molecule capable of replicating and determining the inherited structure of a cell's proteins. |
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| A type of nucleic acid consisting of nucleotide monomers with a ribose sugar and the nitrogenous bases adenine (A), cytosine (C), guanine (G), and uracil (U); usually single-stranded; funcions in protein synthesis and as the genome of some viruses. |
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| One of two families of nitrogenous bases found in nucleotides. Cytosine (C). thymine (T), and uracil (U) are this. |
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| One of two families of hydrogenous bases fould in nucleotides. Adenine (A) and guanine (G) are this. |
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| A sugar (monosaccharide) or one of its dimers (disaccharides) or polymers (polysaccharides). |
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