BIOL 1000 Chapter Notes - Chapter 3: Desmosome, Archaea, Cholesterol

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beigeminnow583

14 Sep 2018

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Continue to looking at the eukaryotic cells, we were getting information about the cytoskeleton, Which direction does kinesin move things-> negative to positive :d. What if cell as a whole, inside out or outside back in-> inside throughout from center of the cell through the surface of the cell. A(cid:374)d protei(cid:374)s that a(cid:272)(cid:272)o(cid:373)plish those (cid:373)o(cid:448)e(cid:373)e(cid:374)ts it"s the gray o(cid:374)e the dy(cid:374)ei(cid:374) We have something called 9+2 complex that"s (cid:449)hat this (cid:272)o(cid:374)figuratio(cid:374) (cid:272)alled, 9 u(cid:374)its o(cid:374) the ouside a(cid:374)d 2 in the center. Then it goes back to the other way. So unlike the bacterial flagellum which is stands in power of boat eukaryotic flagella move it looked like a motion, it looks like both of these operations well the structures do the same thing there are there for movement. They are not evolutionary related, we call them analogous structures (meaning they are doing the same thing but they are not evolved from the same origin that why they called analogous).

Related Questions

1)Describe the directions in which the two motor proteins, kinesin and dynein, travel along a microtubule. Which of the two proteins moves materials towards the Golgi and which moves materials away from the Golgi? Lastly, what is the speed of kinesin dependent on?

2)What are microfilaments crucial for? How do they self-assemble? Which end do they prefer to elongate from?

3)Describe what types of filaments are in each of the bands of the sarcomere. As a muscle fiber is shortened, describe what happens to each of the bands in the sarcomere as the Z lines move inwards.

4)Describe the role of calcium ions in muscle contraction.

5)List the various types of actin-binding proteins

6) A. What are 3 functions of the cytoskeleton?

B.What are the three filaments that compose the cytoskeleton, and what are they composed?

7)How do they see the internal structures of cells in the microscope? What do proteins get labeled with?

8)Myosin II action (Figure 9.61) differs from that of kinesin (Figure 9.15) in that one of the kinesin heads is always in contact with a microtubule, whereas both myosin heads become completely detached from the actin filament. How are these differences correlated with the two types of motor activities in which these proteins engage?

9)If a myofibril were pulled so that the sarcomeres increased in length by approximately 50 percent, what effect would you expect this to have on the contractile ability of the myofibril? Why? What effects would this have on the H, A, and I bands?

10)Because cytoplasmic vesicles are seen to move in both directions within an axon, can you conclude that some microtubules are oriented with their plus end facing the axon terminus and others oriented with the opposite polarity? Why or why not?

1. Kinesin-1 motors can move long distances on microtubule tracks without dissociating. By contrast, myosin II motors in skeletal muscle take only one or a few steps before letting go. What is most likely the difference between these two motors that allow two different types of movement?

A. Differences in length of the stalk of each respective motor allow for differences in step size

B. Differences in ATP versus GTP hydrolysis alter the motor head movement along filaments

C. Actin filaments are smaller in diameter and have less space for movement

D. Binding affinity of the Kinesin-1 motor head to microtubules is high, whereas binding affinity of the myosin II motor head to actin filaments is low

E. Microtubules are larger in diameter and have more space for movement

2. Dynamic instability causes microtubules either to grow or to shrink rapidly. What is the most likely reason for a microtubule to undergo rapid growth?

A. GTP hydrolysis exceeds the rate of heterodimer addition

B. GTP hydrolysis of alpha tubulin causes an outward bend in the heterodimer conformation

C. A low concentration of tubulin heterodimers are in solution

D. Heterodimer addition exceeds the rate of GTP hydrolysis

E. Increased trafficking of microtubule motor proteins favors stability

3. There are no known motor proteins that move on intermediate filaments (IFs). What property of intermediate filaments would most likely explain the lack of motor proteins?

A. Tissue specific expression of IFs prevent a single type of motor protein to evolve over time

B. Lateral bundling of IFs prevent motor movement

C. IFs are less dynamic than microtubules and actin filaments

D. IFs are unpolarized

E. IFs do not bind a nucleotide

4. You discover a mutation that results in less rapid hydrolysis of GTP by the beta-tubulin subunit. What would most likely occur?

A. There would be no change in filament assembly

B. There would be enhanced instability of the microtubule

C. There would be enhanced stability of the microtubule

D. Microtubules would not form

E. There would be enhanced treadmilling

5. Which of the following statements describes common features of cadherins and integrins?

A. They can link to microtubules using specific adapter proteins

B. They mediate heterophillic interactions

C. They achieve high binding affinity through clustering

D. They are responsible for interactions of a cell with the extracellular matrix

E. They are found in the apical plasma membrane of an epithelial cell

6. Intermediate filaments are uniquely non-polar and built by lateral bundling in five steps: 1) synthesis of an alpha-helical monomer, 2) formation of a coiled-coil dimer, 3) formation of a staggered tetramer of two coiled-coil dimers, 4) lateral association of 8 tetramers, and 5) addition of 8 tetramers to a growing filament. At what step is polarity lost?

A. Step 1

B. Step 2

C. Step 3

D. Step 4

E. Step 5

7. Collagenase is an enzyme that breaks peptide bonds in collagen to help destroy extracellular structures. What would be the most likely reason to use collagenase in a cell biology laboratory?

A. Disrupt cadherin interaction with the extracellular matrix

B. Disrupt cell-cell contacts to passage cells in cell culture

C. Dissociate epithelial cells from the underlying basement membrane to separate tissues

D. All of the answers are likely uses for collagenase

E. Lyse cells to expose intracellular proteins and organelles

yellowherring775

not too details, just main points please...

1. What you should know about microtubles

- MT structure, what they are made of

- MT function

- Motor proteins(kinesins&dyneins)

- How kinesins move, coupling to ATP hydrolysis

- Microtubule Organizing Center (MTOC), how MTs are nucleated

- MT dynamics, how it's affected by drugs and MAPs

- dynamic instability and how its linked to GTP/GDP cycle

- cilia/flagella, axoneme structure

- how cilia/flagella move and the role of dynein

-intra-flagellar transport

2. What you should know about actin filaments

- F-actin structure

- F-actin Function

- Motor proteins (myosins)

- Actin dynamics, how it's affected by actin-binding proteins

- the concept of critical concentration

- actin/myosin structure and function in the contezt of muscle

- how muscle contract

- actinomyosin cycle (myosin movement), coupling to ATP hydrolysis

- How cells move and change shape, using actin

3. What you should know about IF

- IF strcuture, what they are made of

- IF function, roles inside and outside cells

- Regulation of nuclear IF in the cell cycle

- be able to compare major features of IF, Actin, and MTs

Bacterial cytoskeleton, that bacteria have proteins that

- polymerize

-affect cell shape, cytokinesis, ect.

- play analogous roles to MT, F-actin

4. what you should know about the cell cycle

- parts of the cell cycle, stages of mitosis

- MPF; how it was identified, what it is made of (cyclin and cdk)

- Universality of cyclin/Cdks (in yeast, frogs, etc.)

-how Cdk activity is regulated (many mechanisms)

- how Cdks function (by phosphorylation)

- how multiple cdks divide their function

- how the spindle is formed and mistakes corrected

- the role of motors and MY dynamics in above

- the tolr of proteolysis in mitotic transitions

- what a checkpoint is

- how checkpoints provide an additional layer of cell cycle regulation in case of damage

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BIOL 1000 Chapter Notes - Chapter 3: Desmosome, Archaea, Cholesterol

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