Exam 1 (Notes)

Question 1

How does cell size affect function?

Answer 1

if it’s too small, it may not contain all the organelles necessary for life

if it’s too big, then there may be communication problems

Question 2

three types of cytoskeleton

Answer 2

actin, microtubules, protein filaments

Question 3

enantiomers

Answer 3

mirror image stereoisomers

Question 4

diastereomers

Answer 4

non-mirror image stereoisomers

Question 5

Hydrophobic Effect

Answer 5

Caging of water molecules by hydrophobic molecules

Question 6

Describe how reactions are favored via enthalpy and entropy.

Answer 6

Reactions are favored by a decrease in enthalpy that coincides with an
increase in entropy

Question 7

examples of amphipathic molecules

Answer 7

micelles and bilayers

Question 8

The Stronger the Acid

Answer 8

the Lower its pKa Value

Question 9

The pKa of an Acid can be Determined by Titration

with a Strong Base

Answer 9

pKa will be the pH where the acid is 50% disassociated

Question 10

Henderson-Hasselbach Equation

Answer 10

pH = pKA + log([A-]/[HA])

Question 11

Normal lab values for arterial blood

Answer 11

pH: 7.35-7.45
pCO2: 35-45 mm Hg
HCO3-: 21-28 mEq/L

Question 12

ABGs

Answer 12

Arterial Blood Gases

Question 13

What does the body do during respiratory

acidosis?

Answer 13

Kidneys increase

retention of HCO3-

Question 14

What does the body do during metabolic acidosis?

Answer 14

Lungs “blow off” CO2

Question 15

Are amino acids acids or bases?

Answer 15

both

Question 16

Amino Acids Acidic Side Chains (pKa)

Answer 16

Histidine (6.0)
Aspartate (3.6)
Glutamate (4.2)

Question 17

Amino Acids Basic Side Chains (pKa)

Answer 17

Tyrosine (10.1)
Cysteine (8.2)
Lysine (10.5)
Arginine (12.5)

Question 18

amino acid structure

Answer 18

a Chiral α Carbon Attached To An Amine, Carboxyl, and Functional “R” Group

Question 19

What does amino acids form when they condense?

Answer 19

peptide bonds

Question 20

motif

Answer 20

recognizable pattern formed from tertiary structure

Question 21

T or F

Hemoglobin has 2-fold Symmetry

Answer 21

T

Question 22

Why use hemoglobin and myoglobin as a model?

Answer 22

very stable, abundant, important, relatively small, easy to manipulate, minimalist system

Question 23

What does a lower Kd value mean?

Answer 23

A higher affinity of ligand for protein

Question 24

What does allostery do to Hb?

Answer 24

Transition for the T state to the R state

Question 25

What are immunoglobulins composed of?

Answer 25

a heavy and light chain that | dimerize to form a tetramer

Question 26

IgM

Answer 26

``` first to be produced in the immune reaction; will usually mature to another type through a process known as class switching ```

Question 27

IgG

Answer 27

Mature form that is very common in the blood

Question 28

IgA

Answer 28

Mature form that is important for mucosal immunity: gut, | reproductive tissues

Question 29

IgE

Answer 29

Mature form that is important for allergic responses

Question 30

rationale drug design

Answer 30

the process of using the known tertiary structure of an active site to design an inhibitor that blocks ligand binding.

Question 31

cell composition

Answer 31

50% protein, 15% carbohydrate, 15% nucleic acid, 10% lipid, 10% misc.

Question 32

relationship between substrate and product via free energy if thermodynamically favorable

Answer 32

product is less than substrate; this releases energy

Question 33

relationship between substrate and product via free energy if thermodynamically unfavorable

Answer 33

product is greater than substrate; this requires energy

Question 34

oxidoreductases class and definition

Answer 34

1. transfer of electrons (hydride ions or H atoms)

Question 35

transferases class and definition

Answer 35

2. group transfer reactions

Question 36

hydrolases class and definition

Answer 36

3. hydrolysis reactions (transfer of functional groups to water)

Question 37

lyases class and definition

Answer 37

4. cleavage bond of C-C, C-O, C-N, or other bonds by elimination, leaving double bonds or rings, or addition of groups to double bonds

Question 38

isomerases class and definition

Answer 38

5. transfer of groups within molecules to yield isomeric forms

Question 39

ligases class and definition

Answer 39

6. formation of C-C, C-S, C-O, and C-N bonds by condensation reactions coupled to cleavage of ATP or similar cofactor

Question 40

prosthetic group

Answer 40

a cofactor in a complex enzyme that is tightly or covalently bound

Question 41

coenzyme

Answer 41

a cofactor in a complex enzyme that is non-covalently bound

Question 42

holoenzyme

Answer 42

complete complex enzyme, protein and cofactor

Question 43

apoenzyme

Answer 43

protein component of a complex enzyme

Question 44

other types of enzyme cofactors

Answer 44

vitamins and metals; Mg, Zi, Mn, Ni, Fe

Question 45

active site

Answer 45

specific region on an enzyme where the substrates are bound

Question 46

How do enzymes bind on substrates?

Answer 46

by multiple weak, reversible attractions such as hydrophobic interactions, ionic interactions, and hydrogen bond

Question 47

binding energy (or bending?)

Answer 47

many weak energy that come together to make a bending energy that can be used to compensate the activation energy; ALL enzymes use this

Question 48

covalent catalysis

Answer 48

transient covalent bond formation between the substrate and functional group at the active site