Answer:
Just think of whats in a forest ecosystem
for example
Water
sunlight
tempreture
Answer:
[K₂CrO₄] → 8.1×10⁻⁵ M
Explanation:
First of all, you may know that if you dilute, molarity must decrease.
In the first solution we need to calculate the mmoles:
M = mmol/mL
mL . M = mmol
0.0027 mmol/mL . 3mL = 0.0081 mmoles
These mmoles of potassium chromate are in 3 mL but, it stays in 100 mL too.
New molarity is:
0.0081 mmoles / 100mL = 8.1×10⁻⁵ M
Answer:
Explanation:
When you form a <em>diluted solution</em> from a mother (concentrated) solution, the moles of solute are determined by the mother solution.
The main equation is:
Then, since the moles of solute is the same for both the mother solution and the diluted solution:
Substitute and solve for the molarity of the diluted solution:
Answer:
expands
Explanation:
Most substances become increasingly compressed when frozen solid, but water is a famous exception.
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.
