WGU C785 unit 2

WGU C785 unit 2 Hydrogen bond Correct Answer: Weak bond interaction Between two molecules amino group Correct Answer: Consists of hydorgen and nitrogen atoms (-NH3+) macromolecules Correct Answer: A giant m ...

WGU C785 unit 2 Hydrogen bond Correct Answer: Weak bond interaction Between two molecules amino group Correct Answer: Consists of hydorgen and nitrogen atoms (-NH3+) macromolecules Correct Answer: A giant molecule in a living organism formed by the joining of smaller molecules: a protein, carbohydrate, or nucleic acid. polymer Correct Answer: a long molecule consisting of many similar or identical building blocks linked by covalent bonds Amino acid Correct Answer: Amino group + Carboxylic acid + R group = Amino acid carboxyl group Correct Answer: A -COOH group, found in organic acids. Coo-, O=C-O- Four classes of biological macromolecules Correct Answer: Proteins, carbohydrates, nucleic acids, lipids SPONCH Correct Answer: Sulfur phosphorous oxygen nitrogen carbon hydrogen polymer Correct Answer: a long molecule consisting of many similar or identical monomers linked together by covalent bonds. R group Correct Answer: a functional group that defines a particular amino acid that makes it a specific protein (20 amino acids) aka side chain Catalyst Correct Answer: Speed up chemical reactions but remain unchanged by the reaction. monomers Correct Answer: repeating units that serve as the building blocks of a polymer enzymes Correct Answer: specialized macromolecules that speed up chemical reactions in cells alpha carbon Correct Answer: the central carbon atom of each amino acid Atomic number Correct Answer: number of protons atomic mass Correct Answer: number of protons plus number of neutrons dehydration synthesis Correct Answer: a chemical reaction in which two molecules become covalently bonded to each other with the removal of a water molecule. amino acid backbone Correct Answer: The structure comprised of the amino group, carboxyl group with a central alpha carbon atom. dehydration reaction Correct Answer: A chemical reaction in which two molecules covalently bond to each other with the removal of a water molecule. Ionic bond Correct Answer: formed when two oppositely charged ions attract Hydrophobic Correct Answer: non polar, afraid of water Disulfide bond Correct Answer: double (di) bond between two Sulfur (sulfide) atoms in cysteine side chains. They stabilize tertiary and quaternary structures of a protein. carbohydrates Correct Answer: Organic compounds composed of carbon, hydrogen, and oxygen in a ratio of one carbon atom to two hydrogen atoms to one oxygen atom. They exist as monosaccharides, disaccharides, and polysaccharides. protein Correct Answer: a macromolecule consisting of one or more polypeptides chains made up amino acids folded and coiled into a specific three-dimensional structure. polar Correct Answer: Amino acid Molecule with partial charges. Mixes with water. covalent bond Correct Answer: formed when the difference in electronegativity between A atoms is equal they then share electrons Polar covalent bond Correct Answer: when electrons are unequally shared between Atoms because they have different electronegativities Functions of proteins Correct Answer: structural support, catalyst, transport, defense, movement, regulation charged Correct Answer: Amino acid has a positive or negative charge hydrophobic effect Correct Answer: (Water Fearing). Tendency of nonpolar (non charged) substances to aggregate (clump together) in water and exclude the water molecules. amino acid Correct Answer: an organic molecule possessing both a carboxyl and an amino group. The monomers of polypeptides. There are 20 different forms. Distinguished by side chains. hydrophobic interactions Correct Answer: Interaction between nonpolar molecules in water. Polypeptide Correct Answer: A single protein chain formed by amino acids bonded together peptide bond Correct Answer: the linkage between amino acids forming a covalent bond between the carboxyl group on one amino acid and the amino group on another, formed by a dehydration reaction. denaturation Correct Answer: loss of a proteins normal 3D structure; can possibly be caused by pH and temperature changes which affect the ionic bonds, hydrogen bonds & hydrophilic interactions Hydrolysis Correct Answer: Peptide bonds can be broken by this...A chemical process that splits a molecule by adding water. ( this happened frequently in the stomach when proteins begin to bee digested into their amino acids) enzyme Correct Answer: a macromolecule serving as a catalyst, a chemical agent that increases the rate of a reaction without being consumed by the reaction. most of them are proteins. Primary Structure Correct Answer: Sequence of amino acids forming a protein or polypeptide chain, the most basic element of its structure. What are the functions of carbohydrates Correct Answer: function as energy source & structure support; examples: simple sugars, and complex polysacchrides, structural suppport examples: cell wall in pant cells, chitin in insects. cellulose Correct Answer: a structural polysaccharide of plant cell walls, consisting of glucose monomers joined by β glycosidic linkages. Quaternary structure Correct Answer: Spatial arrangement of two or more individual polypeptide chains. primary structure Correct Answer: sequence of amino acids in a polypeptide aka amino acid chain secondary structure Correct Answer: Shape formed by hydrogen bonding of amino acid back bone- usually an alpha helix or beta sheet lipids Correct Answer: Large, non-polar organic molecules which do not dissolve in water. - fats, phospholipids, steroids, waxes. disaccharide Correct Answer: a double sugar, consisting of two monosaccharides joined by a glycosidic linkage formed by a dehydration reaction. polysaccharide Correct Answer: a polymer of many monosaccharides, formed by dehydration reactions. tertiary structure Correct Answer: The third level of protein structure; the overall, three-dimensional shape of a polypeptide due to interactions of the R groups of the amino acids making up the chain. Complex folding- critical to proper functioning Secondary structure Correct Answer: Three-dimensional structure of sheets, helices, or other forms taken on by a polypeptide chain, due to electrostatic attraction between neighboring residues. quaternary structure Correct Answer: Results from multiple polypeptide subunits. Held together by R group interactions Subunit Correct Answer: One of the several polypeptide chains that make up a protein hydrophobic effect Correct Answer: Hydrophobic R groups cluster together in the interior of