109/8.56=12.7
50+12.7
V=62.7
Mass= Volume x Density so i divided the mass and density to get the volume. and afterwards i would just add it to the mass to get my final answer
When you heated the can with the bit of water inside and you boiled it over a flame, the water turned to vapor (gas) and the pressure in the inside of the can is different from the pressure on the outside of the can. When you placed the can into a ice water beaker or a container, the can shrunk it's size, decreasing it's mass and density. The can shrunk as a result of the inside pressure being equalized with the outside pressure.
The part where you placed it in the ice bath or container was when the water vapor was forced out of the can.
Q. How many molecules of H2O can be produced from reactants in container below?
A. 3 molecule of molecules H2O will be produced from reactants in container.
<em><u>Explanation</u><u>:</u></em>
There are seven molecules of H2 and three molecule of O2 are there in the container Q, 6 molecules of H2 will react with 3 molecules of O2 to produce 3 molecules of H2O. One molecule of Hydrogen will not take part in reaction and will be present in container Q after then reaction, and the mass in overall reaction is conserved!
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The answer to your question is
D: Unshared Pair
Hope this helps you :))))
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.
