Biology 7.3 Nucleic Acids
Terms in this set (19)
a coiled conformation common in many proteins; it is characterized by a spiral chain of amino acids stabilized by hydrogen bonds in which the resulting structure resembles a spring or helix.
Beta pleated sheet
a structure that occurs in many proteins and consists of two or more parallel adjacent polypeptide chains arranged in a zigzag pattern, so that hydrogen bonds can form between the chains.
ribosomes that are attached to the outer surfaces of endoplasmic reticulum and produce proteins that are used within the plasma membrane or are expelled from the cell via exocytosis.
a biochemical compound, such as hemoglobin, made up of a protein molecule and a non-protein prosthetic group.
alternative structures of the same protein.
a photograph or image of a specimen taken using an electron microscope.
can move about anywhere in the cytoplasm and the proteins they make are free to go anywhere within the cell.
Non-polar amino acid
an alpha-amino acid in which the functional group (R-) attached to the alpha-carbon has hydrophobic properties.
Polar amino acid
an alpha-amino acid in which the functional group (R-) attached to the alpha-carbon has hydrophilic properties.
a polymer of amino acids joined together by peptide bonds.
a group of ribosomes joined by a molecule of messenger RNA containing the genetic information code that is to be translated during protein synthesis.
the linear sequence or order of amino acids of a protein; it determines how the protein will fold into a more advanced structure, such as the unique three-dimensional structure of protein.
the non-protein component of a conjugated protein, for example the heme group in hemoglobin.
the chemical group attached to the alpha carbon in an amino acid that is different for each of the common 20 amino acids found in proteins.
the particular shape of a protein defined by the characteristic three-dimensional arrangement of its constituent polypeptide subunits.
the repetitive folding of the polypeptide backbone of a protein due to the hydrogen bonds formed between the peptides.
the irregular folding of a protein molecule due to the interactions of the R- groups involving hydrophobic interactions, ionic bonds, hydrogen bonds, or disulfide bonds.
the transfer of information from a RNA molecule into a polypeptide, involving the changing of language from nucleic acid to amino acid.
RNA molecules that transport amino acids to ribosomes for incorporation into a polypeptide undergoing synthesis (according to directions coded in the mRNA).