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olga_2 [115]
4 years ago
11

How is hydrogen different from alkali metals?

Chemistry
1 answer:
Irina18 [472]4 years ago
5 0
Hydrogen is different from alkali metals because it also exhibits the properties of inert gas
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If a sloth is traveling at its top speed of 0.067 m/s (0.15 mph), how long does it take the sloth to travel a 11.5 meter tree?
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I think the answer is a: 17mins
7 0
3 years ago
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Having been heated to 800 K , at some point the tank starts to leak. By the time the leak is repaired, the tank contains only ha
Liula [17]

Answer: The temperature of the gas reduced to 400K.

Explanation:

Stated that ; The pressure remains the same, that is initial and final pressure equals 1atm.

Applying Charles Law

V1/T1 = V2/T2

Initial volume V1 = 1

Final volume V2 = 1/2 (halved)

Initial temperature T1 =800K

Final temperature T2 = ?

(1/800) = (1/2)/T2

T2 = 800/2

T= 400K

Therefore, when the volume is halved, the temperature reduced also to half ( 400K)

3 0
3 years ago
The lock-and-key model and the induced-fit model are two models of enzyme action explaining both the specificity and the catalyt
ivolga24 [154]

Answer:

The lock-and-key model:

c. Enzyme active site has a rigid structure complementary

The induced-fit model:

a. Enzyme conformation changes when it binds the substrate so the active site fits the substrate.

Common to both The lock-and-key model and The induced-fit model:

b. Substrate binds to the enzyme at the active site, forming an enzyme-substrate complex.

d. Substrate binds to the enzyme through non-covalent interactions

Explanation:

Generally, the catalytic power of enzymes are due to transient covalent bonds formed between an enzyme's catalytic functional group and a substrate as well as non-covalent interactions between substrate and enzyme which lowers the activation energy of the reaction. This applies to both the lock-and-key model as well as induced-fit mode of enzyme catalysis.

The lock and key model of enzyme catalysis and specificity proposes that enzymes are structurally complementary to their substrates such that they fit like a lock and key. This complementary nature of the enzyme and its substrates ensures that only a substrate that is complementary to the enzyme's active site can bind to it for catalysis to proceed. this is known as the specificity of an enzyme to a particular substrate.

The induced-fit mode proposes that binding of substrate to the active site of an enzyme induces conformational changes in the enzyme which better positions various functional groups on the enzyme into the proper position to catalyse the reaction.

4 0
3 years ago
Is granite rock a compound, element, mixture? Explain
Ghella [55]
It is a <u>mixture</u> of minerals mainly of corps that crystalizes of magma below earths surface.
7 0
3 years ago
For the gas phase decomposition of t-butyl propionate,C2H5COOC(CH3)3 (CH3)2C=CH2 + C2H5COOHthe rate constant at 540 K is 8.90×10
kvv77 [185]

Answer:

The activation energy is 164.02 kJ/mol

Explanation:

Log (k2/k1) = Ea/2.303R × [1/T1 - 1/T2]

k1 = 8.9×10^-4 s^-1

k2 = 9.83×10^-3 s^-1

R = 8.314 J/mol.K

T1 = 540 K

T2 = 578 K

Log (9.83×10^-3/8.9×10^-4) = Ea/2.303×8.314 × [1/540 - 1/578]

1.043 = 6.359×10^-6Ea

Ea = 1.043/6.359×10^-6 = 164020 J/mol = 164020/1000 = 164.02 kJ/mol

6 0
3 years ago
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