1)

Out of the three options you provided, the most accurate statement regarding
microtubule ends is:

The ends differ when it comes to growth dynamics.

This statement reflects the current understanding in cell biology:

Microtubule ends (plus and minus) have distinct properties.

The plus (+) end is more dynamic, exhibiting faster growth (polymerization) and
shrinkage (depolymerization).

The minus (-) end is less dynamic, with slower growth and shrinkage rates.

The other two options have some issues:

Microtubules are asymmetric with respect to the 2 ends because of the asymmetric
structure of the monomer. But the dynamics at both the ends is the same. - This
might be partially true regarding the asymmetric structure of αβ-tubulin subunits,
but the extent of its influence on dynamics at both ends is debatable. Recent research
suggests some differences in dynamics.

Microtubules are symmetric when it comes to the 2 ends. - This is entirely false.
Microtubule ends have well-established differences in dynamics.

2)
I can help you with this! Here are the true statements:

If the polymerization rate is less than the depolymerization rate, the length of Actin
decreases.

If the polymerization rate is more than the depolymerization rate, the length of Actin
increases.

These statements are true because they reflect the balance between the two processes
that determine the overall length of an actin filament:
Polymerization: This process adds actin monomers to the ends of the filament,
leading to an increase in length.

Depolymerization: This process removes actin monomers from the ends of the
filament, leading to a decrease in length.

When the polymerization rate is greater than the depolymerization rate, more
monomers are added than removed, and the filament grows in length. Conversely,
when the depolymerization rate is greater than the polymerization rate, more
monomers are removed than added, and the filament shrinks in length.

The other two statements are incorrect:

If the polymerization rate is less than the depolymerization rate, the length of Actin
increases. (This is the opposite of what actually happens.)

If the polymerization rate is more than the depolymerization rate, the length of Actin
decreases. (This is also the opposite of what actually happens.)

3)
The statement is True.

Here's why:

In chemical reactions, the activation energy refers to the minimum amount of energy
required for the reacting molecules (reactants) to overcome the energy barrier and
form products. The higher the activation energy, the fewer reactant molecules have
enough energy to overcome the barrier and react in a given time.

As a consequence, reactions with a high activation energy will generally proceed at a

slower rate compared to reactions with a lower activation energy.

4)
There are at least 2 different kinds of reactions happening here.

Here’s why the other options are incorrect:

We cannot comment anything about the rate of reactions from the given graph: The
graph does not show the rate of the reactions, only the concentration of the reactants
over time.

The first reaction attains equilibrium much faster than the other reaction: The graph
does not show equilibrium being reached.

The first reaction attains equilibrium much slower than the other reaction: The graph
does not show equilibrium being reached.

Reaction between A and B is faster: The graph does not identify the reactants.

5)
The y-axis shows the “dimensionless concentration” of a substance, likely
representing the concentration relative to a starting concentration.

The x-axis shows “dimensionless time”, which means the time has been scaled to a
unitless value, likely in comparison to an initial time value.

There are three curves on the graph: S, E, and ES.

S likely represents the concentration of the substrate.

E likely represents the concentration of the free enzyme (not bound to substrate).

ES likely represents the concentration of the enzyme-substrate complex.

As discussed previously, the ES complex acts as an intermediate step in enzymatic

reactions. Its formation and dissociation from the substrate (S) can happen relatively
quickly compared to the overall reaction. This faster process is reflected in a steeper
curve for the ES complex concentration (P) on the graph, indicating a lower
timescale compared to the substrate (S) and free enzyme (E).

Therefore, option P, which corresponds to the ES complex concentration, is the most

likely answer.
6)
The statement is False.

In actin filaments, polymerization and depolymerization occur primarily at the ends,

but not equally at both ends. Here's the breakdown:

Barbed End: This end grows faster (polymerizes) and shrinks faster (depolymerizes)
compared to the pointed end. It has a higher affinity for adding new actin monomers.

Pointed End: This end grows slower and shrinks slower compared to the barbed end.
It has a lower affinity for adding new monomers but can still undergo polymerization
and depolymerization.

Therefore, while both ends can undergo these processes, the barbed end exhibits a
higher rate of actin filament dynamics.

7)
The statement is True.

Actin monomers do undergo internal changes in their state besides polymerization

and depolymerization.

Here are some examples of internal changes in actin monomers:

Nucleotide binding: Actin binds to ATP or ADP at a specific site. This nucleotide
bound state affects the affinity of actin for interacting with other molecules and its
ability to polymerize.

Conformational changes: Binding of ATP or ADP, as well as interaction with actin-

binding proteins, can induce conformational changes in the actin monomer
structure. These changes can influence its interaction with other actins and
regulatory proteins.

Modification by covalent attachments: Actin can be modified by attaching chemical

groups like phosphates or acetyl groups. These modifications can alter the function
and interaction of actin within the cell.

Therefore, actin monomers exhibit internal changes beyond just polymerizing and
depolymerizing.
8)