Proteins and Enzymes Flashcards

Flashcards on Proteins and Enzymes

Enzymes

A class of proteins that act as biological catalysts.

Octet Rule

Atoms forming stable molecules have eight electrons in their outer shell.

Covalent Bond

A strong chemical link where electrons are shared between atoms.

Ionic Bond

A bond formed through the attraction between positive and negative charges.

Hydrogen Bonding

Relatively weak attraction between hydrogens and oxygen due to partial charges.

Hydrophobic Interactions

In an aqueous environment, bits of proteins come together due to their hydrophobicity.

van der Waals interactions

Weak interactions that occur between non-polar molecules.

Polar Covalent Bond

Covalent bonds that result in a molecule having a partially negative side and a partially positive side.

Isomers

Molecules with the same constituent parts rearranged in a different way.

Macromolecules

Large molecules that make up a living thing. The four types are proteins, nucleic acids, carbohydrates, and lipids.

Proteins

Polypeptides that fold up within the cell and give that cell its particular functionality.

Nucleic Acids

DNA and RNA

Lipids

Fats, majority of which are found in cell membranes.

Amino Acids

The 20 different chemical constituent parts that form all proteins.

Polypeptide Chain

A polymer formed from lots of amino acids joined together in a chain.

Residue

Another term for individual amino acids.

Hydrophilic Side Chains

Side chains that can hydrogen bond with the aqueous environment.

Hydrophobic

Nonpolar and do not carry a charge on them.

Disulfide Bridge

A covalent link between two amino acids, between the two R groups of cysteine residues.

Peptide Bond

The covalent bond that forms between the carboxylic acid end of one amino acid and the amino group end of an adjacent amino acid.

Hydrolysis

The breaking of covalent bonds using water.

Primary Structure

The sequence of amino acids.

Secondary Structure

Alpha helices and beta sheets that occur because of the hydrogen bonding between the oxygens and the hydrogens that span that covalent bond between the amino acids.

Tertiary Structure

How a protein folds up in three-dimensional space with all of these alpha helices and beta sheets.

Quaternary structure

Individual subunits, individual peptides that come together to give a particular function.