Exam 1 Flashcards

(46 cards)

1
Q

What are the properties of life?

A

-being highly organized
-homeostasis
-reproduction
-growth and development
-transforming energy
-response to stimuli
-adaption to environment

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Who is credited for discovering and coining the term “cell”

A

Robert Hooke

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are the differences between eukaryotes and prokaryotes

A

P = unicellular, absent membrane-bound organelles, DNA in cytoplasm, circular chromosome, binary fission

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What four elements compose about 96% of living matter?

A

carbon, hydrogen, oxygen, and nitrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is a cation and an anion

A

cation = positively charged (ex: sodium)
anion = negatively charged (ex: chloride)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are the four main groups of large organic molecules in cells

A

Carbohydrates, Lipids, Proteins, and Nucleic Acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Why is the carbon atom a versatile building block of molecules

A

contains four valence electrons, which can form covalent bonds with four other atoms - ultimately being able to form many different molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is hydrolysis

A

water is consumed as a reactant to break one larger molecule down into two or more new substances (ex: sucrose broken down to glucose and fructose monomers from water)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is an Anabolic reaction?

A

building of larger complex molecules from smaller simpler ones

requires an input of energy

EX: formation of glycogen from glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is a Catabolic reaction?

A

breaks complex molecules down into smaller components

releases energy

EX: cellular respiration (glucose and oxygen react to yield CO2 and water)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Why do cells not really defy the 2nd law of thermodynamics

A

Cells receive constant input of energy in the form of potential energy in chemical bonds (especially molecules like glucose)

Cells create order at the expense of heat generation - as energy is used, some energy is lost as heat to the environment. This heats up the cell’s surroundings, which adds to disorder

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is a biological example of the first law of thermodynamics

A

use of energy from sunlight in photosynthesis to be converted into chemical energy and stored in the form of glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What are Oxidation and Reduction and what is being oxidized in cellular respiration

A

Oxidation = loss of electrons
Reduction = gain of electrons

OIL RIG

Glucose is being oxidized in cellular respiration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What are the characteristics of enzymes?

A

-not consumed by the reaction
-physically bring the reactant together
-destroy chemical bonds
-provide microenvironment in the active site
-noncovalent bond with reactants

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is an example of a medicine that targets enzymes to treat human disease

A

Gleevec (imatinib)

inhibits the function of the BCR-ABL kinase, being a competitive inhibitor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Why are enzymes called catalysts

A

they speed up a chemical reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Will an exergonic reaction proceed immediately

A

No

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Does spontaneous necessarily mean instantaneous

A

No - spontaneous refers to naturally occurring, not right away

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Why is it beneficial to give someone ethanol if they have been poisoned with methanol

A

Ethanol will compete against methanol for the active site of Alcohol Dehydrogenase, meaning that it is a competitive inhibitor.

20
Q

What are the parts of an amino acid’s structure

A

Amino Group, Carboxyl Group, R Group, Alpha Carbon (central carbon), Hydrogen atom

21
Q

What is the difference between essential and non-essential amino acids

A

Essential = body does not produce, must come from diet

Nonessential = body produces

22
Q

What are the three big categories of amino acids

A

Non-polar (e.g. leucine, glycine)
Polar (e.g. serine, tyrosine)
Electrically Charged (e.g. aspartic acid, lysine)

23
Q

What is Primary Structure

A

-amino acid sequence

24
Q

What is Secondary Structure?

A

polypeptides that can form an alpha-helix or beta-sheet

Hydrogen bonds

Can enclose a hydrophilic region of a protein so that the hydrophobic side chains are on the outisd

25
What are examples of Secondary Structure
Keratin (alpha-helices) Silk (beta sheets) insect/fish antifreeze proteins
26
What is Tertiary Structure
interactions between amino acid side chains covalent, ionic, hydrogen bonds
27
What is Quaternary Structure
multiple subunits combine to form a complete protein structure Disulfide bonds
28
Why do proteins fold
to minimize free energy and to move to a lower energy state
29
What are the importance of disulfide bonds
-added stability, flexibility -found in structural proteins in ECM
30
What is a protein domain
a segment of the polypeptide/protein that folds into an independent compact structure -a protein can have multiple domains
31
What is denaturation and how can it occur
modifying the molecular structure of a protein physical and chemical changes can deactivate a protein - leaves only primary structure through temperature, pH, salt
32
What are the structures that make up an antibody
heavy chain, light chain, disulfide bonds, hyper-variable region
33
How are antibodies used in the lab
to target or mark proteins for visual study (protein localization) and to sort specific proteins (protein purification)
34
What is an Allosteric protein
protein that has two or more conformations *MOST PROTEINS ARE ALLOSTERIC (ex: motor proteins)
35
What does a Kinase do
phosphorylate proteins (add a phosphate group)
36
What does Phosphatase do
dephosphorylates proteins (remove phosphate group)
37
What are GTP-binding proteins
nucleotide triphosphates can be used to regulate protein function EX: odorant receptors
38
Why are misfolded proteins problematic
are prone to aggregation (begin to stack with one another) and cause molecular stress and interfere with cellular function many neurodegenerative disorders
39
What are possible functions for normal prion protein
intracellular signaling cell-cell adhesion maintain myelin sheath of neurons
40
What is an activated carrier molecule
molecule carrying a chemical group in a high-energy linkage, serving as a donor of energy or of the chemical group in many other reactions
41
List 10 proteins and their functions
1. Hemoglobin - transports substances through the body via the blood 2. Actin - structure 3. Myosin - muscle contraction 4. Insulin - hormone signaling 5. Amylase - break down nutrients in food for absorption 6. Antibodies - protection from foreign pathogens or clinical use 7. Collagen - structure 8. Transport Vessicle - transport 9. Transcription Factors - gene regulation 10. Aquaporins - transport of water across the membrane
42
Where does protein synthesis happen
ribosomes
43
How many amino acids are there
20
44
What is Monoclonal vs Polyclonal
M = all recognize same epitope P = all recognize same antigen
45
What is a Noncompetitive inhibitor
binds away from active site, make active site less effective
46
What is a Competitive inhibitor
binds at active site