Explanation:
Both conduction and convection are both forms of heat transfer from one place to another.
- In conduction, there must be contact between two bodies for the process to take place but in convection, the matter moves to transfer heat.
- Conduction mostly occurs in solid substances whereas convection occurs mostly in fluids.
- Heat transfer in conduction is quite slow compared to convection which is much faster.
Example of conduction is heating of iron pot when cooking
Example of convection is the refrigerating system.
Answer : The molecule 
is a polar molecule.
Explanation :
Polar molecule : When the arrangement of the molecule is asymmetrical then the molecule is polar.
Non-polar molecule : When the arrangement of the molecule is symmetrical then the molecule is non-polar.
The given molecule is,
The electronegativities of oxygen and fluorine are different. The molecular geometry of is bent. As, Fluorine is more elctronegative than the oxygen. So, the arrows putting towards the more electronegative element i.e, fluorine. These arrows do not balance each other. Due to this, the asymmetrical arrangement of these bonds makes the molecule polar.
Hence, the given molecule is polar.
Answer:
Boron. The answer is boron.
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.
