Answer:
This means that the isotope of silicon with a mass number of 28 is by far the most common of these three isotopes.
Explanation:
The abundance of Si-28 is 92.23%. Si-29 is 4.68% and Si-30 is 3.09%.
Because most Si atoms have a mass of 28 amu, the average mass of all silicon atoms is very close to 28.
Here is a video which summarizes how to calculate average atomic mass from data about mass and relative abundance.
Answer:
Isotopes of an element are atoms of the same element that have different number of neutrons.
Polar<span> covalent </span>bonding<span> is a type of </span>chemical bond <span>where a pair of electrons is unequally shared between two atoms.</span>
Converting mmHg to atm is solved by division.
Example: Convert 745.0 to atm.
Solution- divide the mmHg value by the 760.0 mmHg / atm.
745 mmHg over 760.0 mmHg/atm
atm value is 0.980263
Now, I am a medical student and we have never had to convert a BP (blood pressure) to atm from mmHg, only ever kPA. SO, I am going to take a guess here and say that when you do the work to solve this, you are going to convert the Systolic (upper #) which is the 145. You should get 0.190789 and then convert the Diastolic (lower #) which is 65. You should get 0.08552632.
So your fraction so to speak should read, 0.190789/0.08552632 or 0.190789 over 0.08552632
(Just to note that is way to low of a BP, although it is irrelevant) Best wishes and good luck. "Remember, never just look for the right answer, look for why it is the right answer!"
Answer:
True
Explanation:
In an uncompetitive inhibition, initially the substrate [S] binds to the active site of the enzyme [E] and forms an enzyme-substrate activated complex [ES].
The inhibitor molecule then binds to the enzyme- substrate complex [ES], resulting in the formation of [ESI] complex, thereby inhibiting the reaction.
This inhibition is called uncompetitive because the inhibitor does not compete with the substrate to bind on the active site of the enzyme.
Therefore, in an uncompetitive inhibition, the inhibitor molecule can not bind on the active site of the enzyme directly. The inhibitor can only bind to the enzyme-substrate complex formed.
