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BIO-330: Cell Biology > Exam 1 > Flashcards

Exam 1 Flashcards

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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

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2
Q

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

A

Robert Hooke

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3
Q

What are the differences between eukaryotes and prokaryotes

A

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

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4
Q

What four elements compose about 96% of living matter?

A

carbon, hydrogen, oxygen, and nitrogen

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5
Q

What is a cation and an anion

A

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

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6
Q

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

A

Carbohydrates, Lipids, Proteins, and Nucleic Acids

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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

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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)

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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

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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)

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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

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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

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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

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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

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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

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16
Q

Why are enzymes called catalysts

A

they speed up a chemical reaction

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17
Q

Will an exergonic reaction proceed immediately

A

No

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18
Q

Does spontaneous necessarily mean instantaneous

A

No - spontaneous refers to naturally occurring, not right away

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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
Q

What are examples of Secondary Structure

A

Keratin (alpha-helices)
Silk (beta sheets)

insect/fish antifreeze proteins

26
Q

What is Tertiary Structure

A

interactions between amino acid side chains

covalent, ionic, hydrogen bonds

27
Q

What is Quaternary Structure

A

multiple subunits combine to form a complete protein structure

Disulfide bonds

28
Q

Why do proteins fold

A

to minimize free energy and to move to a lower energy state

29
Q

What are the importance of disulfide bonds

A

-added stability, flexibility
-found in structural proteins in ECM

30
Q

What is a protein domain

A

a segment of the polypeptide/protein that folds into an independent compact structure

-a protein can have multiple domains

31
Q

What is denaturation and how can it occur

A

modifying the molecular structure of a protein

physical and chemical changes can deactivate a protein - leaves only primary structure

through temperature, pH, salt

32
Q

What are the structures that make up an antibody

A

heavy chain, light chain, disulfide bonds, hyper-variable region

33
Q

How are antibodies used in the lab

A

to target or mark proteins for visual study (protein localization) and to sort specific proteins (protein purification)

34
Q

What is an Allosteric protein

A

protein that has two or more conformations

*MOST PROTEINS ARE ALLOSTERIC
(ex: motor proteins)

35
Q

What does a Kinase do

A

phosphorylate proteins (add a phosphate group)

36
Q

What does Phosphatase do

A

dephosphorylates proteins (remove phosphate group)

37
Q

What are GTP-binding proteins

A

nucleotide triphosphates can be used to regulate protein function

EX: odorant receptors

38
Q

Why are misfolded proteins problematic

A

are prone to aggregation (begin to stack with one another) and cause molecular stress and interfere with cellular function

many neurodegenerative disorders

39
Q

What are possible functions for normal prion protein

A

intracellular signaling
cell-cell adhesion
maintain myelin sheath of neurons

40
Q

What is an activated carrier molecule

A

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
Q

List 10 proteins and their functions

A
  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
Q

Where does protein synthesis happen

A

ribosomes

43
Q

How many amino acids are there

A

20

44
Q

What is Monoclonal vs Polyclonal

A

M = all recognize same epitope
P = all recognize same antigen

45
Q

What is a Noncompetitive inhibitor

A

binds away from active site, make active site less effective

46
Q

What is a Competitive inhibitor

A

binds at active site

BIO-330: Cell Biology (6 decks)

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