Biochemistry C785 WGU module 2 with correct answers

Biochemistry C785 WGU module 2 amino group - correct answer Consists of hydorgen and nitrogen atoms (-NH3+) carboxyl group - correct answer A -COOH group, found in organic acids. 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 alpha carbon - correct answer the central carbon atom of each amino acid amino acid backbone - correct answer The structure comprised of the amino group, carboxyl group with a central alpha carbon atom. Hydrophobic - correct answer non polar, afraid of water polar - correct answer Amino acid Molecule with partial charges. Mixes with water. charged - correct answer Amino acid has a positive or negative charge Polypeptide - correct answer A single protein chain formed by amino acids bonded together peptide bond - correct answer The chemical bond that forms between the carboxyl group of one amino acid and the amino group of another amino acid by dehydration ( In which a water molecule is removed, C-N bond) 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) Residue - correct answer Remaining portion of amino acids after linked by peptide bonds ( how R groups get their name) N-terminus - correct answer the end of a polypeptide or protein that has a free amino group ( usually on the left) C-terminus - correct answer the end of a polypeptide or protein that has a free carboxyl group ( usually on the right) 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 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 quaternary structure - correct answer Results from multiple polypeptide subunits. Held together by R group interactions subunit - correct answer Each polypeptide chain that is part of a larger protein hydrophobic effect - correct answer Hydrophobic R groups cluster together in the interior of a protein to minimize their contact with water. ( this stabilizes the folded polypeptide backbone) induces aggregation hydrophobic interactions - correct answer Slight attraction (very weak) when non polar groups are close together and result in hydrophobic protein core and hydrophilic proteins on the surface ( globular or spherical proteins- i.e. hemoglobin) hydrogen bond - correct answer Bonds between hydrogen atom and oxygen atom of another amino acid side chain ( between non-polar amino acids, ends in C-H's) ionic bond - correct answer Forms between 2 oppositely charged side chains of the charged amino acids ( AKA salt bridge or ion pair) disulfide bond - correct answer 2 cysteine R groups come together to form a covalent disulfide bond between the 2 sulfur atoms Polar bond - correct answer a covalent bond in which electrons are shared unequally ( ends in OH or NH or SH or H) aggreggate - correct answer Hydrophobic molecules Clump together in a disorderly way Chaperones - correct answer Helper molecules that assist in protein folding of a newly made polypeptide degradation - correct answer Protein is broken down back into individual amino acids and recycled into other proteins. Denaturation - correct answer loss of normal shape of a protein due to heat(hydrophobic interactions) , changes in pH(ionic/hydrogen bonds), high salt concentrations( ionic/hydrogen bonds) or reducing agents ( disulfide bonds) catalyst - correct answer substance that speeds up the rate of a chemical reaction and remain unchanged from the reaction ( this is what enzymes are) activation energy - correct answer Energy needed to get a reaction started Substrate - correct answer A specific molecule on which an enzyme works. active site - correct answer The binding platform part of an enzyme for its specific substrate. Substrate bonding affinity - correct answer Attraction of substrate to the active site of an enzyme phosphorylation - correct answer Kinase- Attachment of a phosphate group of a polar amino acid to modify a protein to regulate enzyme activity Dephosphorylation - correct answer Phosphatases- Removal of a phosphate group of a polar amino acid to modify a protein to regulate enzyme activity allosteric site - correct answer A site on an enzyme other than the active site, to which non competitive inhibitors bind, changing the shape and activity of the enzyme. feedback inhibition - correct answer A kind of reversible non competitive inhibitor that regulates the rate and affects many metabolic pathways ( when the final product has built up enough it signals an enzyme in the front of the cycle to cease the reaction) Competitive inhibitor - correct answer Molecule that competes with substrate to bind to the active site induced fit - correct answer Active site conforms slightly to better accommodate the substrate ( hugs the substrate)