Organic Chemistry Test 4 (Ch 18,19 and 20) – Flashcards
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Select the true statement:
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You expect water to have a higher boiling point that octane
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Aldehydes are reduced to form what type of compound?
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A primary alcohol
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The boiling point of a branched alkane is generally ____ that of the straight chain alkane with the same number of atoms
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Lower than
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Why do carboxylic acids have higher boiling points than similar alcohols or aldehydes?
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They form dimers that are relatively stable
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Acid hydrolysis of an ester produces
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A carboxylic acid and an alcohol
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When butanoic acid and NaOH react in a neutralization reaction, what is the name of the salt product?
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Sodium butanoate
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Over the counter antacids like Tums help heartburn because
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Tums contain a base which neutralizes stomach acid in a neutralization reaction
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What alcohol was used to form propyl butanoate, which is an ____?
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1-propanol, ester
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Carboxylic acids ionize in water to produce
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Carboxylate ion and hydronium ion
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Which statement is not true:
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All lipids contain a fatty acid
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In the fluid mosaic model that describes plasma membranes...
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Two layers of glyercophospholipid molecules have their nonpolar sections oriented to the inside of the membrane
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The name of the reaction that occurs when a fat reacts with sodium hydroxide is:
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Saponification
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What are the product of hydrolysis of a traicylglycerol molecule?
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Glycerol and three fatty acids
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A triacylglycerol that is solid at room temperature is called an oil
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False
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Trans fats are regarded as the best fats for human health
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False
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Olive oil is a triacylglycerol that contains a high percentage of saturated fatty acids
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False
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The family of biomolecules called lipids are all soluble in organic solvents
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True
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Some fatty acids are called essential because all organisms on earth can produce them
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False
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Waxes contain an ester functional group
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True
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A carboxylic acid can be neutralized with HCL
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False
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Methanol and ethanol are common alcohols used to produce waxes
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False
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Long chain carboxylic acids are also known as fatty acids
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True
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Products like Crisco are formed by hydrogenation of vegetable oils
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True
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Amines are organic compounds that contain what element?
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Nitrogen
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Amines are derivatives of what compound?
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Ammonia
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What is a primary amine?
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One carbon group or none, are bonded to the nitrogen atom
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What is a secondary amine?
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Two carbon groups are bonded to the nitrogen atom
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What is a tertiary amine?
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Three carbon groups are bonded to the nitrogen atom
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What is the amine ending?
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-amine
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What is the substituent name for amines?
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Amino
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What is the name of a benzene ring with an amine?
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Aniline
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Is the N-H bond polar or nonpolar?
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Polar, because Nitrogen is strongly electronegative
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What kind of amines do not participate in hydrogen bonding?
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Tertiary amines
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Which is more electronegative: Nitrogen or Oxygen
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Oxygen
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Do amines or alcohols have higher boiling points?
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Alcohols because N is less electronegative compared to O
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Which type of amine has the highest boiling point?
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Primary amines
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Are amines soluble in water?
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Yes, because they participate in hydrogen bonding
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Up to how many carbons are soluble in an amine?
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6 carbons
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Do amines react as acids or bases?
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Bases
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What type of base is an amine?
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Bronsted-Lowry Base
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Do bases accept or give hydrogens?
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Accept to have a plus charge
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What type of reaction is specified to be between an acid and a base, and what is the product?
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Neutralization reaction, amine salt
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What is a heterocyclic amine?
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An organic compound that contains 1 or more hydrogen in a ring of 5 or 6 atoms other than just carbon
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What is an alkaloid?
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A physiologically active amine produced by plants
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What is an amide?
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Derivatives of carboxylic acids and amines; the hydroxyl group on a carboxylic acid is replaced by a nitrogen from the amine
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What is the formation of amides called?
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Amidation reaction
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What is an amidation reaction?
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When carboxlyic acids are heated with amines
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What types of amines undergo amidation reactions?
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Primary and secondary amines
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Up to how many carbons is an amide soluble?
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5 carbons
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What is an amino acid?
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Building blocks of proteins
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What is a protein?
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A group of amino acids linked together
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How many different amino acids are used in humans?
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20 amino acids
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What are classifications of amino acids?
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Non-polar, polar, acidic ,and basic
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What makes an amino acid non-polar?
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Contains an alkyl group, or an aromatic
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What makes an amino acid polar?
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Contains a hydroxyl, thiol, or an amide
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What makes an amino acid acidic?
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Contains a carboxylic acid group
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What makes an amino acid basic?
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Contains an amino group
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What is a zwitterion?
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An ion with no overall net charge, but has charges present on a molecule
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What is an isoelectric point or pI?
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The ph of an atom when the charge is zero, or when it is a zwitterion
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Do amino acids act as acids or bases?
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Both, acids donate hydrogen and bases accept hydrogen
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What is a peptide bond?
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An amide bond that forms between the -COO group of one amino acid and the -NH3 group of another amino acid (formed in amidation reactions)
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What is the N-terminus?
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The end of a peptide bond with a free amino
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What is the C-terminus?
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The other end of a peptide bond with a free carboxyl
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What are oligopeptides?
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Molcules with up to 20 amino acids
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What are polypeptides?
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Molecules with more than 20 amino acids
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Over 50 amino acids is referred to as what?
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A protein
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How many levels of structure is there for proteins?
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Four
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What is the primary structure?
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The order of amino acids
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What is the secondary structure?
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When amino acids form hydrogen bonds within polypeptides between 2 peptide chains; otherwise understood as the way amino acids near each other are arranged in space
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What are types of secondary structure?
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Alpha helix, and beta sheet
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What is an alpha helix?
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A right-handed corkscrew held in place by hydrogen bonds between N-H of one amino acid and the O of the C doubled bonded to the O four amino acids away
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What is a beta-pleated sheet?
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Polypeptides held together side by side through hydrogen bonds, backbone is extended
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What is the tertiary structure?
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The way secondary structures fold up to make the protein
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What is the quaternary structure?
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Interactions of more than one polypeptide chain
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What are hydrophobic interactions?
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interactions between non polar groups
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What are hydrophilic interactions?
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attractions between the aqueous environment and polar and or ionic side chains; found on the outer surface of a proteins 3D structure
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What are salt bridges?
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These are ionic bonds between basic and acidic side chains that hold positive or negative charges at pH 7
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What are hydrogen bonds?
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Formed between amino acids that have side chains that can h-bond
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What are disulfide bonds?
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covalent bonds formed between the -SH gorup of two cysteines
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What is a globular protein?
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A protein that is compact, with a spherical shape because secondary structures fold on top of each other
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What are fibrous proteins?
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Have a long, thin, fiber like shape (contains alpha and beta keratins)
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What is hydrolysis?
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The splitting of an amide in the presence of an acid or bas; the reverse of peptide bond formation; disrupts primary structure
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What is denaturation?
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A disruption of bonds that hold secondary, tertiary, or quaternary structure; does not disrupt primary structure only unfolds the protein
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What is a catalyst?
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An agent that speeds up a chemical reaction by lowering activation energy
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What is an enzyme?
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A biological catalyst
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What is activation energy?
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The minimum amount of energy required to initiate a chemical reaction
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What is the ending for an enzyme?
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-ase
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Occasionally and enzyme will end in what?
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-in
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How many classes of enzymes are there?
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6
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What are the six classes of enzymes?
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Oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases
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What type of enzyme catalyzes oxidation-reduction?
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Oxidoreductases
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What type of enzyme transfers groups of atoms?
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Transferases
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What type of enzyme catalyzes hydrolysis?
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Hydrolase
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What type of enzyme adds atoms or removes atoms to form double bonds?
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Lyases
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What type of enzyme rearranges atoms?
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Isomerases
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What type of enzyme uses ATP to combine small molecules?
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Ligases
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What is a substrate?
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The molecule that goes into an enzymes active site
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What is an active site?
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The part of the enzyme that interacts with the substrate; usually a small pocket on the edge of the protein
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What is an absolute enzyme?
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Enzymes that catalyze one type of reaction for a single substrate
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What is a group enzyme?
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Enzymes that catalyze one type of reaction for similar substrates
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What is a linkage enzyme?
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Enzymes that catalyze one type of reaction for a specific type of bond
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What is the enzyme substrate complex? (ES)
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When a substrate bonds with the active site
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What are the two models of substrate binding to the active site?
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Lock and key model, induced fit model
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What is the lock and key model?
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Older view that the substrate fits directly into he active site because it has the right shape, if it has the wrong shape the enzyme will not work; views that the active site is rigid and not flexible
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What is the induced fit model?
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Newer view that the active site adjusts to fit the shape of the substrate, working together to acquire the proper geometry
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What is the activity of an enzyme?
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How fast an enzyme catalyzes or how fast it turns substrate into product
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What is temperature?
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The average kinetic energy of a population
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What is the prime temperature for enzyme to catalyze?
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37 degrees, over 50 it is not possible, nor when it is too cold
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What occurs when the pH goes below optimal?
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Acid has been added and the protein has unfolded
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What occurs when the pH goes above optimal?
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Base has been added and the protein has unfolded
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What is the optimum pH for most enzymes?
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7.4
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What is the optimum pH for pepsin and trypsin?
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1.5-2
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What happens when more enzymes are added?
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Reaction rates increase
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What is saturation?
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When all enzyme active sites are full
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What is an inhibitor?
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Molecules that cause enzymes to lose activity
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What are the two classes of enzymes?
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Reversible and irreversible
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What is a reversible enzyme?
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Allows enzymes to regain their activity after acting with an inhibitor
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What is an irreversible enzyme?
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Denys enzymes to regain their activity
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What is a competitive enzyme?
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A reversible inhibitor that looks like the substrate and can bind in the active site of an enzyme
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What is non-competitive enzyme?
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A reversible inhibitor that does not resemble the substrate and does not compete for the active site but rather binds somewhere besides the active site on the enzyme and distorts shape
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What makes an inhibitor irreversible?
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It covalently bonds to the enzyme, losing all activity permanently
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What is a cofactor?
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Outside help provided by small molecules or metal ions
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What is a coenzyme?
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A cofactor that is an organic molecule, includes vitamins
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What makes a vitamin water soluble?
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Containing a polar group, eliminated from the body through urine
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What makes a vitamin fat soluble?
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Long chain carbon groups, limited hydrogen bonding opportunities, not eliminated from the body
