I cant see it maybe post it again?
Answer :
Example of polar covalent molecules H-O-H(water), ammonia
Explanation:
The presence of intermolecular Hydrogen bonding makes the boiling point of water unexpectedly high, and the polar covalent nature makes it dissolve polar solute/compound
Answer:
1.332 g.
Explanation:
- We can use the general law of ideal gas: <em>PV = nRT.</em>
where, P is the pressure of the gas in atm.
V is the volume of the gas in L.
n is the no. of moles of the gas in mol.
R is the general gas constant,
T is the temperature of the gas in K.
- At the same T and P and constant V (1.0 L), different gases have the same no. of moles (n):
<em>∴ (n) of CO₂ = (n) of C₂H₆</em>
<em></em>
∵ n = mass/molar mass
<em>∴ (mass/molar mass) of CO₂ = (mass/molar mass) of C₂H₆</em>
mass of CO₂ = 1.95 g, molar mass of CO₂ = 44.01 g/mol.
mass of C₂H₆ = ??? g, molar mass of C₂H₆ = 30.07 g/mol.
<em>∴ mass of C₂H₆ = [(mass/molar mass) of CO₂]*(molar mass) of C₂H₆</em> = [(1.95 g / 44.01 g/mol)] * (30.07 g/mol) =<em> 1.332 g.</em>
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A. BeCl2 sp2
Also when you get the chance, could you mark me brainliest?
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.