Category - Definitions

Query - What definition best describes the term below?

Reversal

Category - Term Recognition

Query - What term does the description below refer to?

(Terms are shown on left, descriptions in middle, figures on right)

amino acid | An organic acid containing an amino group on the carbon immediately adjacent to the carboxyl group. | Figure 5.3 | Aminoacyl-tRNA | tRNA molecules carry amino acids to the ribosomes to be incorporated into polypeptide chains in translation. tRNAs linked to amino acids are called ***. | Figure 5.19 | Aminoacyl-tRNA synthetases | Enzymes that catalyze the covalent linkage of amino acids to specific tRNAs. | Figure 5.19 | Anticodon loop | A loop at one end of a tRNA molecule that is complementary to the codon of a mRNA. | Figure 5.20 | Asymmetric center | A carbon atom that has four different substituents attached to it; such a group cannot be superimposed on its own mirror image and therefore can occur in two enantiomers. | Figure 5.5 | Chiral | With respect to a molecule or other object, the property of being nonsuperimposable on its mirror image. | Figure 5.5 | Cystine | The amino acid cysteine frequently forms disulfide bonds with other cysteines. The resulting disulfide form of cysteine is called *** |  | Dipeptide | A molecule containing two amino acids joined by a peptide bond. | Figure 5.8 | Disulfide bond | A direct covalent bond between two sulfur atoms. | Figure 5.15 | Enantiomers | Stereoisomers that are nonsuperimposable mirror images of each other. Also called optical isomers. | Figure 5.5 | Enzymes | Proteins that catalyze chemical reactions. |  | Genetic code | The code by which the nucleotide sequence of a DNA or RNA molecule specifies the amino acid sequence of a polypeptide. It consists of three-nucleotide codons that either specify a particular amino acid or tell the ribosome to stop translating and release the polypeptide. | Figure 5.16 | Leader Sequence | For a protein, a short N-terminal hydrophobic sequence that causes the protein to be translocated into or through a cellular membrane. | Figure 5.21 | Oligopeptide | A chain of several amino acids linked by peptide bonds. |  | Peptide | General term for a molecule containing peptide bonds. |  | Peptide bond | The bond that links successive amino acids in a peptide. It consists of an amide bond between the -carboxyl group of one amino acid and the -amino group of the next. | Figure 5.21 | Polyampholytes | Molecules which contain multiple acidic and basic groups. |  | Polypeptide | A chain of many amino acids linked by peptide bonds. |  | Primary structure of a protein | Refers to the sequence of amino acids in a protein. |  | Proteases | Enzymes that cleave peptide bonds in a polypeptide. Many show specificity for a particular amino acid sequence. |  | Proteins | Mature polypeptide chains. Differ from polypeptides in being folded into the proper 3D configuration and/or modified. May consist of one or more polypeptide chains. | Figure 5.20 | Stereoisomers | Molecules containing a center of asymmetry can exist in different 3D isomeric forms. *** refers to the different forms. | Figure 5.5 | Tetrapeptide | A chain of four amino acids linked by peptide bonds. | Figure 5.9 | Translation | The synthesis of a polypeptide under the direction of an mRNA, so that the nucleotide sequence of the mRNA is converted into the amino acid sequence of the protein. | Figure 5.20 | Zwitterion | A molecule with equal numbers of positive and negative charges - thus the net charge is zero. | Figure 5.2 Category - Structures Query - What is the structure of the molecule below? Reversal Category - Molecules

Query - What is the name of the molecule with the structure below?

(molecule name on left, structure in middle, figures on right)

L-Alanine | Structure |  | L-Arginine | Structure |  | L-Asparagine | Structure |  | L-Aspartic Acid | Structure |  | L-Cysteine | Structure |  | L-Glutamine | Structure |  | L-Glycine | Structure |  | L-Histidine | Structure |  | L-Isoleucine | Structure |  | L-Leucine | Structure |  | L-Lysine | Structure |  | L-Methionine | Structure |  | L-Phenylalanine | Structure |  | L-Proline | Structure |  | L-Serine | Structure |  | L-Threonine | Structure |  | L-Tryptophan | Structure |  | L-Tyrosine | Structure |  | L-Valine | Structure |  | -Alanine | Structure |  | D-Alanine | Structure |  | -Aminobutyric acid | Structure |  | D-Glutamic acid | Structure |  | L-Homoserine | Structure |  | L-Ornithine | Structure |  | Sarcosine | Structure |  | L-Thyroxine | Structure |  | o-Phosphoserine | Structure |  | 4-Hydroxyproline | Structure |  | -Hydroxylysine | Structure |  | -Carboxyglutamic acid | Structure |  | Cyanogen bromide | Structure |  | Methyl thiocyanate | Structure |

Category - Enzymes

Query - What enzyme/reagent has this activity?

Reversal

Category - Reactions

Query - What catalytic activity does the enzyme below have?

(activity description on left, enzyme/reagent on right)

Protease that cleaves peptide bonds on carboxyl side of lys or arg residues (not adjacent to proline) | Trypsin | Protease that cleaves peptide bonds on carboxyl side of tyr, phe, leu, ile, val, trp, and his at high pH (not adjacent to proline) | Chymotrypsin | Protease that cleaves peptide bonds on carboxyl side of phe, leu, others (not adjacent to proline) | Pepsin | Protease that cleaves peptide bonds on carboxyl side of arg (not adjacent to proline) | Thrombin | Protease that cleaves peptide bonds on carboxyl side of arg, lys or the next amino acid beyond phe | Papain | Protease that cleaves peptide bonds on carboxyl side of lys, ala, tyr, gly | Bromelain | Protease that cleaves peptide bonds on amino side of tyr, phe, leu, ile, val, trp, and his(not adjacent to proline) | Thermolysin | Protease that cleaves peptide bonds with little specificity | Subtilisin | Protease that cleaves peptide bonds on amino side of carboxyterminal amino acids (not adjacent to proline) | Carboxypeptidase A | Chemical agent that cleaves peptide bonds on carboxyl side of methionine residues | Cyanogen bromide