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25 Cards in this Set

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Covalent bond
a chemical bond in which electrons are shared between two atoms
Denaturation
destruction of the folding properties of a protein leading (usually) to loss of biological activity
Enantiomer
one form of a molecule that is the mirror image of another form of the same molecule
Glycosidic bond
a type of covalent bond that links sugar units together in a polysaccharide
Hydrogen bond
a weak chemical bond between a hydrogen atom and a second, more electronegative element, usually an oxygen or nitrogen atom
Isomers
two molecules with the same molecular formula but which differ structurally
Lipid
glycerol bonded to fatty acids or other hydrophobic molecules by ester or ether linkage. Often contain other groups, such as phosphate as well
Macromolecule
polymer of covalently linked monomeric units
Molecule
two or more atoms chemically bonded to one another
Nonpolar
possessing hydrophobic (water-repelling) characteristics and not easily dissolved in water
Nucleic acid
DNA or RNA
Nucleoside
a nucleotide without its phosphate group
Nucleotide
a monomer of a nucleic acid containing a nitrogen base (adenine, guanine, cytosine, thymine, or uracil), a molecule of phosphate, and a sugar, either ribose (in RNA) or deoxyribose (in DNA)
Peptide bond
a type of covalent bond linking amino acids in a polypeptide
Phosphodiester bond
a type of covalent bond linking nucleotides together in a polynucleotide
Polar
possessing hydrophilic characteristics and generally water-soluble
Polymer
a chemical compound formed by polymerization and consisting of repeating units called monomers
Polynucleotides
a polymer of nucleotides bonded to one another by phophodiester bonds
Polypeptide
a polymer of amino acids bonded to one another by peptide bonds
Polysaccharide
a polymer of sugar units bonded to one another by glycosidic bonds
Primary structure
in an informational macromolecule, such as a polypeptide, the precise sequence of monomeric units
Protein
a polypeptide or group of polypeptides that form a molecule of specific biological function
Quaternary structure
in proteins, the number and types of individual polypeptides in the final protein molecule
Secondary structure
the initial pattern of folding of a polypeptide or a polynucleotide, usually dictated by opportunities for hydrogen bonding
Tertiary structure
the final folded structure of a polypeptide that has previously attained secondary structure