Exam 1

Question 1

Malaria

Answer 1

Plasmodium falciparum
People who are carriers for sickle cell and have one faulty gene are immune.
People with two faulty genes have sickle cell, and people with two normal genes are at risk for malaria.

Question 2

Cell Cycle

Answer 2

G1: gap 1, RNA/protein synthesis
G0: resting phase
S: DNA synthesis
G2: gap 2, RNA/protein synthesis
M: mitosis, sister chromatids separate.

Question 3

Bonds that Form Secondary Structure

Answer 3

Alpha helix: intramolecular H bonds.
Beta sheets: intermolecular H bonds.

Question 4

Secondary Structure Motifs (3)

Answer 4

Coiled-Coil: 2 alpha helices intertwined; myosin.
Helix-Loop-Helix (EF Hand): 2 helices connected by a loop; calmodulin.
Zinc-Finger: Alpha helix and Beta sheet with Zinc; transcription factors.

Question 5

Neutrophil Extracellular Traps (NET)

Answer 5

Happens when neutrophils get overwhelmed; they use cell cycle proteins to release NETs and trap pathogens.

Question 6

Chaperones vs. Chaperonin

Answer 6

Chaperones are a class of proteins that promote folding.
Chaperonins are a type of chaperone protein that forms folding chambers for proteins.

Question 7

Gel Electrophoresis

Answer 7

Method of separating proteins based on size.
Proteins start on negative end and travel towards positive.
Smallest proteins will travel farthest.

Question 8

Two-Dimensional Gel Electrophoresis

Answer 8

Separates molecules based on charge and mass.
Provides greater resolution than either procedure done alone.

Question 9

Gel Filtration Chromatography

Answer 9

Separation of proteins by size.
Gel contains beads that have small canals in them. The smaller proteins will get caught in the canals and the larger proteins will pass through the gel more quickly.

Question 10

Ion Exchange Chromatography

Answer 10

Proteins are sent through positively charged beads to catch anionic proteins and elute cationic proteins. Then a salt solution is added to elute anionic proteins.

Question 11

X-Ray Crystallography

Answer 11

Can determine 3D structure.
Have to dessicate to crystalize, which can damage the structure.
Larger proteins are harder to crystallize.

Question 12

Cryoelectron Microscopy (Cryo EM)

Answer 12

Uses frozen samples to visualize 3D structure.
The specimen is frozen in its native state and doesn’t need dyes or fixatives (PRO).
The sample has to be frozen so quickly that no ice crystals form.
Not good for smaller molecules.

Question 13

Peroxisomes

Answer 13

Produce H2O2 thru beta oxidation and then break down excess using catalase.

Question 14

Golgi Complex

Answer 14

Modifies and sorts ER products.
3 Regions: cis (entry), medial, and trans (exit).

Question 15

Smooth and Rough ER

Answer 15

Smooth: lipid synthesis and detoxification.
Rough: protein and membrane synthesis.

Question 16

3 Types of Cytoskeleton Proteins

Answer 16

Microfilaments: thinnest; microvilli, sarcomeric units, and dendrites.

Microtubules: thickest; cilia, flagella, axons, spindle fibers.

Intermediate Filaments: connecting organelles, cell-cell and cell-matrix adhesions.

Question 17

SEM and TEM

Answer 17

SEM: electron beam directed at surface of sample releasing a secondary beam that is received by a detector.
TEM: electron beam passed through the sample to a detector on the other side; better resolution.