Unit 2, 3, & 5 (Amino acids, Proteins, Hemoglobin)

Question 1

an alpha carbon is…

Answer 1

the central carbon atom of every amino acid

Question 2

an amino acid consists of…

Answer 2

an amine group, carboxyl group, and an R group with a central (alpha) carbon atom

Question 3

how many different amino acid groups are there?

Answer 3

20

Question 4

the amino group, carboxyl group, and central carbon make up…

Answer 4

the amino acid backbone

Question 5

the amine group of an amino acid consists of…

Answer 5

hydrogen and nitrogen atoms (NH3+)

Question 6

the carboxyl group of an amino acid consists of…

Answer 6

one carbon and 2 oxygen atoms (COO-); has lost its hydrogen

Question 7

Nonpolar (hydrophobic) amino acids all have what type of “R” group build?

Will a nonpolar amino acid interact/bond with a polar amino acid?

What type of interaction?

Answer 7

carbons (C) bonded to hydrogens (H) atoms (weak bonds).

No, nonpolar amino acids will only interact/bond with other nonpolars.

Hydrophobic interactions.

Question 8

Nonpolar (hydrophobic) amino acids are disrupted by…

Answer 8

heat

Question 9

Polar, uncharged amino acids contain…and form this type of bond____, unless 2 cystine (sulphur) amino acids bond, then the bond is a…

Answer 9

sulphur (S), oxygen (O) or nitrogen (N) bonded to hydrogen (H).

hydrogen bond (strong); biochem is a SON of a

disulfide bond.

Question 10

Polar amino acids (except cystine) hydrogen bonds are disrupted by…

Cystine disulfide bond is broken by…

Answer 10

pH and salt changes.

a reducing agent.

Question 11

The amino acid _____ can produce a _____ bond, the strongest, and requires a ______ agent to disrupt the interaction.

Answer 11

cystine; disulfide; reducing

Question 12

Charged amino acids will consist of ___, ___, or ___ bonded to hydrogen (H) and form ____ bonds disrupted by…

Answer 12

sulphur (S), oxygen (O), or nitrogen (N)

ionic

pH and salt changes.

Question 13

Peptide bonds hold together amino acids at what level of protein structure?

Answer 13

Primary

Question 14

Tertiary protein structure is noted when ___ ___ and ___ ___ attractions cause ___ folding and a ___D shape.

Answer 14

a-helix, b-pleated sheets

distant

3

Question 15

The 4 R-group interactions are…

Answer 15

Hydrophobic interactions (nonpolar)

Hydrogen bonds (polar)

DIsulfide bonds

Ionic bonds (charged)

Question 16

The 4 R-group interactions can stabilize what levels of protein folding?

Answer 16

Tertiary and Quaternary

Question 17

A protein structure consisting of more than one amino acid chain with subunits…

Answer 17

Quaternary protein structure

Question 18

Hg and antibodies are made up of ____ protein structure, and the body can replace a ____ instead of the entire structure if needed.

Answer 18

quaternary

subunit

Question 19

____ folding stabilized by ___ bonded amino acids spiralizing and pleating is indicative of Secondary protein structure.

NH’s and CO’s repetitively ____.

Answer 19

Local

hydrogen

stack.

Question 20

Aggregation of proteins occurs d/t ____ ____ between nonpolar amino acids.

Answer 20

hydrophobic interactions

Question 21

Enzymes lower the ____ ____ to catalyze reactions.

Answer 21

activation energy

Question 22

_____ inhibitors attach somewhere other than the active site, alter the shape/confirmation of the enzyme and active site, making the active site nonfunctional.

Another name for these inhibitors is ____

Answer 22

Noncompetitive

Allosteric (allo = other)

Question 23

Competitive inhibitors ____ with substrates mimicking their behavior and attach at the ____ ____ of an enzyme.

Answer 23

compete

active site

Question 24

What is the substrate of aldolase B, and how do you know that?

Answer 24

F1P

Substrate is always before the arrow of the reaction.

Question 25

Identify the enzymes. How do you know that?

Answer 25

Fructokinase and Aldolase B They end in *ase*, and in pathway examples, they are above the arrows.

Question 26

Can F1P be a product?

Answer 26

Yes, it's the product of *fructokinase*. Substrates can be *products* as well as *substrates*.

Question 27

What would happen if aldolase B didn't function?

Answer 27

DHAP and Glyceraldehyde would not be produced, but F1P would accumulate.

Question 28

How could we increase the amount of DHAP and glyceraldehyde produced?

Answer 28

Increase the amount of F1P, but to do that, you have to increase the intake of fructose.

Question 29

Identify the products in this pathway. Identify the substrates/reactants.

Answer 29

Question 30

What does the blunt line in this pathway represent?

Answer 30

The F molecule is causing *inhibition* to the enzyme in step 2. Also called *feedback inhibition*, d/t a product of the pathway inhibiting a step in the same pathway.

Question 31

Answer 31

C is the substrate for E4, which helps convert C to X. If you inhibit E1, C is unable to be produced, therefore X is decreased or not made.

Answer 32

E3 catalyzes substrate D to F, and F inhibits E4. When E3 is inhibited, product F can't be made. If F isn't made, E4 is no longer inhibited, so E4 will then increase the production of X.

Question 33

What is an *Allosteric site?*

Answer 33

It is the binding site on *Allosteric enzymes* - enzymes that have an additional site for an effector to bind to, as well as the active site.

Question 34

Kinase

Answer 34

An enzyme that catalyzes the transfer of phosphate groups - a substrate phosphate donating molecule) to the product, which is a phosphate acceptor. These are known as phosphorylation types of reactions.

Question 35

Phosphatase

Answer 35

An enzyme that catalyzes the opposite of the kinase types of reactions. Phosphatase removes a phosphate group from the substrate. These reactions are known as the dephosphorylation types of reactions.

Question 36

# Define affinity Which has higher affinity for O2, Hemoglobin or Myoglobin?

Answer 36

How "sticky" the protein is to oxygen. Myoglobin - bc it stores O2 The higher the curve, the higher the affinity of that protein.

Question 37

What is the function of hemoglobin? How many subunits does it have? How many heme groups, iron, and O2 molecules does it carry?

Answer 37

Pick up O2 in the lungs and deliver it to hypoxic tissues. 4 Each subunit binds to 1 heme group = 4 Each heme group associates with 1 iron (Fe) = 4 Each iron binds to 1 O2 molecule = It can carry and transport 4 O2 molecules

Question 38

What is myoglobins function? How many subunits? How many heme groups, iron, and O2 molecules does it store?

Answer 38

Store O2 in the muscles. 1 1 subunit binds to 1 heme group The 1 heme group associates with 1 iron The 1 iron binds to the 1 O2 molecule it can store.

Question 39

How does carbon monoxide (CO) cause poisoning? What color are pt's with CO poisoning?

Answer 39

It binds to Hg subunits O2 sites, but more strongly, has a higher affinity for hemoglobin, and bc Hg has cooperativity, O2 comes to the other open sites. Then CO stays and holds the other 3 O2 hostage. Therefore Hg will readily pick up O2, but CO prevents it from dropping it off to hypoxic tissues. Pink

Question 40

How do changes in pH affect the ability of hemoglobin to bind (affinity) or release O2?

Answer 40

Higher pH (Left shift) = higher affinity to O2, will bind to O2 more readily in lungs, low H+ Lower pH (Right shift) = lower affinity to O2, will release O2 easily in muscles d/t high H+ and low O2

Question 41

Answer 41

Answer 42

Question 43

How do changes in pH affect hemoglobin's structure?

Answer 43

Low pH (high H+) = Hg tense (muscle) High pH (low H+) = Hg relaxed (lungs)

Question 44

The amount of concentrated H+ ions in a solution is known as \_\_\_.

Answer 44

pH

Question 45

An acidic solution has a pH of... A basic solution has a pH of...

Answer 45

\< 7 \> 7