Chem Exam 4

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Last updated 2:49 PM on 4/30/26
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39 Terms

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lipids

organic molecules that are not water soluble.

  • no specific functional group

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4 basic categories of lipids

fats and waxes, complex lipids, steroids; prostaglandins, leukotrienes, thromboxanes

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fats and waxes

fatty acids, 12-20 carbon monocarboxylic acids

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unsaturated fatty acids

have double bonds, can undergo chemistry to metabolize easier.

  • melting points are lower than saturated fat melting points.

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all natural unsaturated fatty acids are

cis unsaturated fatty acids

  • have a lower melting point

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polyunsaturated fats

more desirable because lower melting point and more reactive

  • means its easier to metabolize

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triglycerides

glycerol backbone with 3 fatty acids

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soap

glycerol and the sodium salts of fatty acids.

created when a triglyceride reacts with a base such as NaOH

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linoleic and linolenic fats

essential fats

  • alpha and omega fatty acids

  • need from outside sources

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complex lipids

phospholipids and glycolipids

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phospholipids

have a glycerol or sphyngocine backbone

  • both include a phosphate group

Phosphate group adds dual solubility

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glycolipids

have a sphingocine backbone and a sugar group

also possesses dual solubility

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steroids

4 rings: 3 six membered rings, 1 five membered ring

ex. cholesterol

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Cholesterol

liver breaks down HDL into bile salts.

building block of steroids and sex hormones

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bile salts

amphipathic molecules that act as detergents

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prostaglandins

mediate fever and pain

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leukotrienes

trigger inflammation, bronchioconstrictors (athsma)

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thromboxanes

promote blood clotting, vasoconstrictor

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proteins

polyamides, come from a carboxylic acid reacting with an amine (dehydration rxn)

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Amino acids

20 common

all are water soluble and have a high melting point

react with itself due to zwitteronic forces

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amino acid structure

alpha carbon, amine group, carboxyl group, and R group

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primary structure of protein

amino acid sequence, amide bonding through dehydration

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2º structure

folding patterns: alpha helix or beta pleated sheet

  • occur through hydrogen bonding between two amino acids in the backbone

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3º structure of proteins

interactions with the R group

  • ionic bond

  • hydrophobic interactions

  • hydrogen bonding

  • disulfide linkage

  • metal ion coordination

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4º structure of protein

consists of more than one amino acid chain

ex. hemoglobin

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protein function

  1. enzymes

  2. immunoglobulins

  3. transport proteins

  4. regulatory proteins (insulin)

  5. structural proteins

  6. movement

  7. receptor proteins

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denaturing proteins

ruining a proteins shape, done by denaturing bonds in the 2º or 3º structures.

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denaturing methods

  1. adding an acid or base

  2. [O] or [H]

  3. adding salts or metals

  4. physically mixing it

  5. heat

  6. adding organic compounds or solvents

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enzymes

proteins found in the cell that are responsible for catalyzing chemical reactions

  • super specific, usually 1 enzyme for a given chemical reaction.

  • make reactions faster by 108 - 1020

  • remain unchanged

  • each cell contains > 3000 enzymes

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lock and key method

reactant is the substrate and the active site on the enzyme is what it’s interacting with

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induced fit model

the enzyme is always moving but it accommodates the substrate as the substrate approaches.

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What can alter the active site

pH and temp.

most enzymes optimal pH is 5-8.

  • if not at optimum, the enzymes will denature and no longer work

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cofactors

inorganic enzyme helpers that make for proper enzyme activity.

  • minerals

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coenzymes

organic helpers for proper enzymatic activity

ex. vitamins

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competitive enzyme inhibition

the inhibitor blocks the active site, not allowing the substrate access to it, thus no reaction.

adding more substrate can override and increase the rate of reaction

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non-competitive inhibition

interact at a different spot on the enzyme, changes the shape of the active site.

  • substrate cannot interact and no reaction occurs

  • adding more substrate does not increase the rate of reaction.

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allosteric/non-competitive regulation

inhibitor

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proenzyme/zymogen

group on/group off inactive group preventing enzyme from working

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feedback control

one of the products acts as an inhibitor.