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Binghamton University - BIOL 311 - Test 4 – RVB Final Exam and Actual Detailed Answers Updated.

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Cytosekeleton - Answer Network of filaments that run throughout the cytoplasm, is dynamic and not static, can be a target for cancer (microtubules) What does the cytoskeleton do - Answer Gives the cell its shape and aids in movement, guide for vesicular transport and orientation of organelles where is Internal cytoskeleton - Answer Specific to Eukaryotes 3 Major components - Answer 1.) Actin filaments (microfilaments, smallest) 2.) Intermediate filaments (Medium size) 3.) Microtubules (largest) Type of intermediate filaments - Answer Keratin filaments that interconnect desmosomes Where are actin filaments found - Answer In cortex and microvilli Microtubules - Answer Involved in mitosis and in non-dividing cell often radiate out from a MTOC (microtubule organizing center) Experiment with force of filaments - Answer Increasing force, measure when it breaks and how much it stretches, intermediate filaments are the toughest and don't break How much of proteins do actin filaments make up - Answer 10% in muscle cells, 1-5% in normal cells, most abundant protein in muscle cells Molecular weight of actin filaments - Answer 42000 - G-actin (globular) How many actin genes are there - Answer 6 in humans that each encode an isoform Alpha actin - Answer Associated with contractile structures Beta actin - Answer Front or leading edge of moving cells

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Binghamton University - BIOL 311 -
Test 4 – RVB Final Exam and Actual
Detailed Answers 2025-2026 Updated.
Cytosekeleton - Answer Network of filaments that run throughout the cytoplasm, is dynamic
and not static, can be a target for cancer (microtubules)



What does the cytoskeleton do - Answer Gives the cell its shape and aids in movement,
guide for vesicular transport and orientation of organelles



where is Internal cytoskeleton - Answer Specific to Eukaryotes



3 Major components - Answer 1.) Actin filaments (microfilaments, smallest)

2.) Intermediate filaments (Medium size)

3.) Microtubules (largest)



Type of intermediate filaments - Answer Keratin filaments that interconnect desmosomes



Where are actin filaments found - Answer In cortex and microvilli



Microtubules - Answer Involved in mitosis and in non-dividing cell often radiate out from a
MTOC (microtubule organizing center)



Experiment with force of filaments - Answer Increasing force, measure when it breaks and
how much it stretches, intermediate filaments are the toughest and don't break



How much of proteins do actin filaments make up - Answer 10% in muscle cells, 1-5% in
normal cells, most abundant protein in muscle cells



Molecular weight of actin filaments - Answer 42000 - G-actin (globular)



How many actin genes are there - Answer 6 in humans that each encode an isoform



Alpha actin - Answer Associated with contractile structures



Beta actin - Answer Front or leading edge of moving cells

,Gamma actin - Answer Accounts for filaments in stress fibers



F-actin - Answer consists of units G-actin arranged in a tight helix, binds either ATP or ADP



How to examine F to G actin change - Answer In vitro, by changing the concentrations of F-
actin and ion concentration (add Mg, K, or Na - induce polymerization)



Myosin S1 - Answer Can be used to decorate F-actin and looks like a series of arrow heads
pointing in one direction -> suggests polarity at ends



Polarity of F-actin - Answer Has a (+) and (-) end that are different, (+) is barbed, (-) is
pointed



How can F-actin polarity be monitored (3) - Answer 1.) Viscometry

2.) Sedimentation

3.) Fluorescence



3 phases of F-actin - Answer 1.) Nucleation

2.) Elongation

3.) Steady State



Steady state - Answer Shows no net change in length, solution has reached the critical
concentration



Critical concentration of G-actin - Answer The concentration of actin at which there is no
change in length at (+) or (-) ends



Difference between CC of (+) and (-) - Answer (+) = 0.12 uM

(-) = 0.60 uM



5 fold difference = G-actin adds 5 times faster at (+) end than (-) end



Capping in vivo vs in vitro - Answer In vivo = see "capping" of one end so the rates are
different, in vitro = theoretically possible for actin filaments to treadmill

, Treadmill - Answer Occurs at CC values intermediate between the (+) and (-) ends values,
responsible for some cell movement



What can toxins do - Answer Alter actin polymerization



Cytochalasin D - Answer Fungal product that inhibits polymerization by binding to (+) end
(inhibits F-actin)



Phalloidins - Answer Toxins from mushroom (Amanita/Angel of Death) that promote
polymerization



Use of phalloidins and remedy - Answer Remedy - eat lots of raw meat to saturate and can
be used to fluorescently tag actin



What regulates actin polymerization in vivo - Answer Actin-binding proteins



Thymosin beta4 - Answer Regulates G-actin polymerization, calculations suggest all G-actin
should be F-actin but 40% is in G form



What specifically does Thymosin beta4 do - Answer Sequesters ATP-G-actin and maintains
active G-actin pool, more Thymosin Beta4 more G-actin



Profilin - Answer Regulated G-actin polymerization, binds to ADP-actin in a 1:1 ratio



How does Profilin promote F-actin assembly - Answer Encouraging the ATP for ADP exchange
(only protein known to do this), aids in addition of monomers to the (+) end of F-actin



Cofilin - Answer Binds to filaments containing ADP-actin, inducing them to fragment and
thus enhancing depolymerization, one of the severing proteins



Proteins to sever actin filaments and where did discovery come from - Answer Gelsolin and
cofilin, discovery from amoeba during movement (cytosol moves from center to edge)



How do severing proteins work - Answer Cap the (+) end and prevents addition of units, (-)
end shortens and increases the solubility of filaments



CapZ - Answer Binds to the (+) end of actin and prevents addition or loss of units

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