According to the law of conservation of mass, the amount of BARIUM present of the reactants is the same as the amount present in the products (the precipitate).
(11.21 g BaSO4) / (233.4 g/mol BaSO4) = 0.0480 mol BaSO4 and original barium salt
(10.0 g) / (0.0480 mol) = 208.3 g/mol
So it must have been BaCl2, because the molar mass of Barium is 137 which leave 71 grams left. Since Barium is a +2 charge, it means the atom next to it must be twice. Chlorine mass is 35, which twice is 71
Answer:
The Mitochondria
Explanation:
Mitochondria are membrane-bound cell organelles that generate most of the energy required to power the cell's organic chemistry reactions. Energy created by the mitochondria is kept in a tiny molecule known as adenosine triphosphate (ATP).
Answer:
It depends on whether the setting is hot or cold .-.
Explanation:
Answer: 7.07 grams
Explanation:
To calculate the moles :
According to stoichiometry :
1 mole of 
require 1 mole of 
Thus 0.052 moles of will require=
of
Thus is the limiting reagent as it limits the formation of product and is the excess reagent.
As 1 mole of give = 1 mole of 
Thus 0.052 moles of give = of
Mass of 
Thus 7.07 g of will be produced from the given masses of both reactants.
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.
