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Artemon [7]
3 years ago
13

What happens to acceleration when the mass goes up or down?

Chemistry
2 answers:
Slav-nsk [51]3 years ago
5 0

Answer:

If you increase the mass at a given force the rate of acceleration slows. Therefore, mass is inversely proportional to acceleration.

Explanation:

Thats the answer I need brainliest PLEASE jk.

Tom [10]3 years ago
5 0

Answer:

Explanation:

Force = mass * acceleration

So if the mass increases the acceleration goes down and if it decreases the acceleration increases.

You might be interested in
.Name a letter never used in any element symbol?​
marta [7]

Answer:

Q

Explanation:

Q does not appear in any official element names. Temporary element names, such as ununquadium, contain this letter.

8 0
3 years ago
You collect 552 mL of argon gas at 23.0 C. What volume will the gas occupy at 46.0C if the pressure remains constant?
taurus [48]

Answer:

1027.9 mL

Explanation:

Formula P1 x V1 / T1 = P2 x V2 / T2

Fill in what you know

Pressure is constant so no need to put that in making the formula

V1 / T1 = V2 / T2

Voulme 1= 950 mL

Volume 2= ?

Temperature 1 = 25 C

Temperature 2 = 50 C

Explanation:

Formula P1 x V1 / T1 = P2 x V2 / T2

Fill in what you know

Pressure is constant so no need to put that in making the formula

V1 / T1 = V2 / T2

Voulme 1= 950 mL

Volume 2= ?

Temperature 1 = 25 C

Temperature 2 = 50 C

8 0
2 years ago
(a) At what substrate concentration would an enzyme with a kcat of 30.0 s−1 and a Km of 0.0050 M operate at one-quarter of its m
Dmitrij [34]

The missing graph is in the attachment.

Answer: (a) [S] = 0.0016M

              (b) Vmax = 3V; Vmax = \frac{3V}{2}; Vmax = \frac{11V}{10}

              (c) Enzyme A: black graph; Enzyme B = red graph

Explanation: <u>Enzyme</u> is a protein-based molecule that speed up the rate of a reaction. <u><em>Enzyme</em></u><em> </em><u><em>Kinetics</em></u> studies the reaction rates of it.

The relationship between substrate and rate of reaction is determined by the <u>Michaelis-Menten</u> <u>Equation</u>:

<u />V=\frac{V_{max}[S]}{K_{M}+[S]}<u />

in which:

V is initial velocity of reaction

Vmax is maximum rate of reaction when enzyme's active sites are saturated;

[S] is substrate concentration;

Km is measure of affinity between enzyme and its substrate;

(a) To determine concentration:

0.25V_{max}=\frac{V_{max}[S]}{0.005+[S]}<u />

<u />0.25V_{max}(0.005+[S])=V_{max}[S]<u />

<u />0.00125+0.25[S]=[S]<u />

0.75[S] = 0.00125

[S] = 0.0016M

For a Km of 0.005M, substrate's concentration is 0.0016M.

(b) Still using Michaelis-Menten:

<u />V=\frac{V_{max}[S]}{K_{M}+[S]}<u />

Rearraging for Vmax:

V_{max}=\frac{V(K_{M}+[S])}{[S]}

(b-I) for [S] = 1/2Km

V_{max}=\frac{V(K_{M}+0.5K_{M})}{0.5K_{M}}

V_{max}=\frac{V(1.5K_{M})}{0.5K_{M}}

V_{max}= 3V

(b-II) for [S] = 2Km

V_{max}=\frac{V(K_{M}+2K_{M})}{2K_{M}}

V_{max}=\frac{V(3K_M)}{2K_M}

V_{max}=\frac{3V}{2}

(b-III) for [S] = 10Km

V_{max}=\frac{V(K_{M}+10K_M)}{10K_M}

V_{max}=\frac{V(11K_{M})}{10K_{M}}

V_{max}=\frac{11V}{10}

(c) Being the affinity between enzyme and substrate, the lower Km is the less substrate is needed to reach half of maximum velocity.

Km of enzyme A is 2μM and of enzyme B is 0.5μM.

Enzyme B has lower Km than enzyme A, which means the first will need a lower concnetration of substrate to reach half of Vmax.

Analyzing each plot, notice that the red-coloured graph reaches half at a lower concentration, therefore, red-coloured plot is for enzyme B, while black-coloured plot is for enzyme A

<u />

3 0
3 years ago
The Ksp of cobalt(II) hydroxide, Co(OH)2, is 5.92 × 10-15. Calculate the molar solubility of this compound.
Dima020 [189]
The Ksp of cobalt(II) hydroxide is equal to [OH-]2[Co2+]=5.92*10-15. And [OH-]=2[Co2+]=2*[Co(OH)2](dissolved). So the molar solubility of this compound is 1.14*10-5 M.
5 0
4 years ago
What causes temporary hardness of water?<br>​
Andreas93 [3]

Answer:

the water hardness caused by the presence of the dissolved bicarbonate minerals

8 0
3 years ago
Read 2 more answers
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