Answer:
The solute is the substance that is being dissolved,
Explanation:
A solution is a homogeneous mixture consisting of a solute dissolved into a solvent .
Answer:
Double replacement reaction.
Explanation:
The Na and Ag atoms both (double) trade places (replacement) with each other.
Answer:
The simulated 1H NMR spectrum for ethyl acetate is shown in the drawing attached.
Explanation:
To construct this NMR it is necessary to identify the essential components that can produce resonance peaks.
Two main groups can be identified, the acetyl group containing a sub-component (CH3) capable of producing a resonance peak, and the ethyl group containing two components (CH2 and CH3) each of which can produce on its own its own resonance peak.
Answer:
Polar
Step-by-step explanation:
Electronegativity increases from <em>left to right</em> in the Periodic Table.
Cl is further right than C (both tinted pink) in the portion of the Periodic Table below.
Cl is <em>more electronegative</em> than C, so the Cl has a partial negative charge and the C has a partial positive charge.
The C-Cl bond is polar.
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.