Exam 1 Review Flashcards

1
Q

What are some advantages and disadvantages of light microscopy as compared to electron microscopy?

A

In light microscopy, the cell will not die or be mutilated during the process, but there are convolution, resolution, and transparent cell issues.

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

What are basic features of a cell?

A
  1. cell membrane and cytosol
  2. A way to store information (DNA)
  3. A way to make components (ex. Ribosomes make protein)
  4. A way to create fuel (ATP)
  5. Means of copying information for reproduction
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What has been a driving force in our understanding of cells?

A

microscopy

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

What are some ways features within a cell can be labeled in light microscopy?

A

stains/dyes, specific antibodies coupled to a fluorophore, genetic fusions between a gene encoding a protein of interest and a fluorescent protein

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

How does fluorescence work? Be able to explain the following: fluorophore, excitation wavelength, emission wavelength

A

1) How does fluorescence work? Be able to explain the following: fluorophore, excitation wavelength, emission wavelength

First, a fluorophore is a fluorescent molecule that is fused with the DNA in a target cell. This will allow the cell to reflect a specific color light. All color light waves come from the light source. All colors are filtered through an excitatory filter and then the one color remaining is reflected by a beam splitting mirror except for the excitatory color (wavelength). This will light up fluorophores that react with that color. The sample reflects the wanted color onto the eyepiece, which is called the emission wavelength which is filtered through the emissions filter.

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

What is “resolution” in the context of microscopy? What is the numerical resolution limit of light microscopy? In basic terms, what aspect of the nature of light causes this limitation?

A

Resolution is the ability to tell 2 objects apart from each other. The numerical limit is 200 nm. The diffraction limit of light causes this limitation.

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

What are super-resolution light microscopy techniques designed for?

A

Super-resolution light microscopy techniques are designed to overcome the resolution limitations of light microscopy. Some approaches have increased the resolving power by a factor of 10 (20 nm)

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

The diffracted light produces a “convoluted” signal can be…

A

deconvolved to reduce blurring effect

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

What has evolved to form a fluorophore from an amino acid?

A

Fluorescent proteins like green fluorescent protein (GFP) have evolved to form a fluorophore from amino acids and can be molecularly modified to improve the signal.

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

How can a fusion protein be used to study the localization of a protein in a living cell by fluorescence microscopy?

A

The DNA sequence for a fluorescent protein can be fused to the DNA sequence for another protein of interest. The modified gene is introduced into the cell and the location of the fusion protein can be observed and tracked.

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

What does “confocal” fluorescence microscopy do differently than non-confocal fluorescence microscopy? What is an optical section?

A

Confocal microscopes exclude light above and below the focal plane, capturing “optical sections”*
Two features: 1. Laser excitation, 2. Pinhole aperture

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

What is special about electron microscopy?

A

Resolution of electron microscopy is not limited by its wave-like nature (as its wavelength is much smaller than light). EM can achieve resolutions >1,000x higher than light microscopy.

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

What would be different about the images of a cell when taken by TEM vs SEM?

A

In TEM, the image will be 2D and it will have been created by electrons that are passing through the sample to create the image.
In SEM, the image will be 3D and it will be the electrons reflecting off the sample.

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

Role of the Nucleus

A

Information store of the cell. Dark spots are the subdomain where ribosomes are made.

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

Role of the Rough ER

A

encloses lumen in membrane compartments. has docked ribosomes that move proteins through ER membrane. Produces most membrane proteins.

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

Role of the Smooth ER

A

Smooth appearance and has no ribosomes. Synthesis of lipids & steroids. Regulation of calcium concentrations. Detoxification of drugs and poisons

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

Role of the Golgi Appartatus

A

has flattened membrane-enclosed disks. Cis (close to ER) and trans (close to membrane) Golgi. It sends out proteins and lipids to the lysosomes, the membrane, and the vesicles. Abundant in plants. Has enzymes for breaking down proteins.

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

Role of the mitochondria

A

generate ATP from sugar, fatty acids, and ketone bodies in the cytosol with aerobic respiration.

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

Role of the lysosome

A

contain enzymes for degradation and recycling of biomolecules. it must be packaged because it is an oxidizing environment.

20
Q

Role of the peroxisome

A

contain hydrogen peroxide and are sites of certain chemical reactions such as inactivation of toxins. Peroxisomes are the sites in which yeast and plants break down fats. Animal cells also do this in their mitochondria.

21
Q

Role of the chloroplast

A

endosymbiosis as well.

22
Q

Role of transport vesicles

A

storage and movement around the cell

23
Q

Process of endocytosis

A

moving things into the cell

24
Q

Process of exocytosis

A

moving things out of the cell

25
Q

Explain how amyloid structures form and discuss some of the consequences of their improper folding and aggregation.

A

A group of proteins that form beta‑pleated sheets which are resistant to proteolysis. When amyloids are misfolded, they form aggregates of hundreds and more monomeric peptides into long fibers. These form amyloid plaques that accumulate in brain tissues and are toxic and Contribute to neurodegenerative disorders - Alzheimer’s and Huntington’s disease - Not contagious from one individual to another

26
Q

Describe the structure of a glycerol-containing phospholipid. What is the backbone and what three things does this attach to?

A

Fatty acid, glycerol, phosphate group, choline. the backbone is a hydro-carbon chain a part of the fatty acid.

27
Q

What is meant by the term “amphipathic?”

A

This means the molecule has a hydrophillic and a hydrophobic end

28
Q

What is endosymbiosis?

A

Early eukaryotes acquired their mitochondria through endocytosis of an aerobic bacteria, bring the more efficient aerobic metabolism to eukaryotes. Previously, they were strictly anaerobic and largely consumed prokaryotes for energy

29
Q

Actin Filaments Basics:

A

abundant in muscle cells where they are used in contraction

30
Q

Intermediate filaments

A

provide structural support in animal cells

31
Q

What is the relationship between the number of valence electrons and the number of covalent bonds an atom can form? What does this suggest for carbon, nitrogen and oxygen?

A
  • Most stable/lowest energy state
  • Valance shell filled
  • Octet rule: H and He exceptions to the rule
    -Covalent bond: When atoms share electrons
    This suggests that C, N, and O bond well with many other molecules.
32
Q

Be able to describe what a covalent bond means, and how a single covalent bond differs from a double/triple covalent bond with respect to freedom of movement.

A

Covalent bonds are sharing of electrons, single bonds allow for movement and double/triple bonds allow for less movement.

33
Q

Why are some molecules polar while others are non-polar? Include the role of electronegativity.

A

Electrons are often shared unequally in covalent bonds, forming a polar molecule with partial charges.
Electronegativity: the degree to which an element tends to gain electrons and form negative ions in chemical reactions

when two electronegative atoms “share” a hydrogen atom. This is an attraction of opposite partial charges.

34
Q

What is an ionic bond? Do these form between atoms with partial or full charges?

A
  • Know that water able to separate sodium and chloride ions to dissolve salt
  • Ionic is a type of chemical bond where atoms are bonded together by the attraction between opposite charges. Bond between metal and non-metal
35
Q

How do Van der Waals interactions work? Dipole-dipole charges

A

weak interactions between nearby atoms, and are formed by slight induced dipoles (uneven charge) as their electrons repel one another. The only reason we know its happening is millions happen at a time.

36
Q

Understand the hierarchy of bond strength and its strength in water.

A

Covalent (377 kJ/mole) > ionic (12.6 kJ/mole) > hydrogen bonds (4.2 kJ/mole) > Van der Waals (.4 kJ/mole)

37
Q

What do amino acid side chains do?

A

the different amino acid side chains can contribute to the non-covalent interactions which occur within a protein to determine its final, most stable structure, as well as the interactions the protein can form with other proteins or molecules.

38
Q

Define a protein’s primary, secondary, tertiary, and quaternary structures.

A

Primary: amino acids joined by peptide bonds
Secondary: alfa helix or beta pleated sheets
Tertiary: Can find - α-Helix or β-pleated sheets or a combination of both
Quaternary: when 2 or more folded polypeptide chains (subunits) come together into one complex

39
Q

Explain how amyloid structures form and discuss some of the consequences of their improper folding and aggregation.

A

A group of proteins that form beta‑pleated sheets which are resistant to proteolysis. When amyloids are misfolded, they form aggregates of hundreds and more monomeric peptides into long fibers. These form amyloid plaques that accumulate in brain tissues and are toxic and Contribute to neurodegenerative disorders - Alzheimer’s and Huntington’s disease - Not contagious from one individual to another

40
Q

What is a prion? What are the consequences of the change from alpha-helices to beta-pleated sheets in prion structure?

A

A normal structural component of the nervous system Proteinatous material (without RNA or DNA) - yet contagious among individuals When misfolded they form a subclass of amyloids Normal prion has alpha-helical is converted into beta‑pleated isoform Amyloid fibers are formed by the beta‑sheet stabilization of the abnormally folded proteins. Causes Creutzfelt-Jakobs disorder (neurodegenerative)

41
Q

Explain how noncovalent interactions and specific protein conformation play in allowing proteins to recognize and bind specifically to their ligands.

A

protein conformation, acts for a slot that the ligand can fit into. Puzzle piece with analogy. Pretend the pieces has magnets on it as well.

42
Q

Explain how and why feedback control might be used to regulate enzyme activity.

A

feedback control allows regulation because it allows a product of a system loop around and halt production of that system by binding to a site on the protein that is not an active site.

43
Q

Explain how the binding of a ligand at a regulatory site can alter the activity of a protein or enzyme, allosteric regulation.

A

Allosteric regulation of a protein means that a ligand or other protein will bind to it and produce a subtle change in the proteins structure. * This commonly can switch an enzyme on or off, or change its catalytic rate.

44
Q

Explain the difference between a tumor suppressor and an oncogene in light of loss of heterozygosity and dominant negative effects

A

Tumor supressor: Its gene product suppresses tumorigenesis (slows down the cell cycle) * All you need is one good copy * If heterozygous (one copy is good and one is bad) - OK

Oncogene: Its gene product promotes cell division * All you need is one bad copy, it is dominant negative

45
Q

Describe the structure of a glycerol-containing phospholipid. What is the backbone and what three things does this attach to?

A

Fatty acid, glycerol, phosphate group, choline. the backbone is a hydro-carbon chain a part of the fatty acid.

46
Q

What is meant by the term “amphipathic?”

A

This means the molecule has a hydrophillic and a hydrophobic end

47
Q

What is the difference between saturated and unsaturated lipid tails?

A

Saturated lipids have single carbon bonds and unsaturated lipids have a double carbon bond which makes the bond ridged.