Answer:
1.) To convert between grams and moles, you would use the substance's molar mass. To go from grams to moles, divide the grams by the molar mass. 600 g58.443 g/mol = 10.27 mol of NaCl. It has been found that 1 mol of any gas at STP (Standard Temperature and Pressure = 0 °C and 1 atm) occupies 22.4 L
Answer:
C₂Cl₄
Explanation:
To know if free rotation around a bond in a compound is possible, we need to see the structure of the compound (picture in attachment).
In single bonds, which are formed by σ bonds, the atoms are not fixed in a single position, and free rotation is permitted.
Double and triple bonds are formed by a σ bond and one or two π bonds, respectively. These bonds do not allow rotation, since it is not possible to twist the ends without breaking the π bond.
The chloroethylene (C₂Cl₄) has two carbons with an sp2-sp2 hybridization, they are bonded together by a double bond. <u>Free rotation on this bond is not possible, because six atoms, including the carbon atoms, doubly bonded and the four chlorine atoms bonded to them, must be on the same plane. </u>
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.
