A Plate Boundaries and Movement Lab Report is a report that shows the records of all the data relating to the movement of Plate Boundaries and their movements.
<h3>What are Plates in this context?</h3>
A tectonic plate is also described or referred to as a Lithosperic Plate. In Geography, it is described as a slab of rock that is not shaped regularly.
In most cases, it comprises continental and oceanic lithosphere.
<h3>Why is it crucial to record the movement of plates and their boundaries?</h3>
Plate Boundaries and their movement are largely linked to volcanic activities and earthquakes. This means that they can be used to predict when any of the above-mentioned events may happen.
Learn more about plate boundaries at:
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Answer:
% sodium= 13.6 % sodium
% carbon= 35.5 % carbon
% hydrogen= 4.7% hydrogen
% nitrogen = 8.3% nitrogen
% oxygen = 37.8 % oxygen
Explanation:
To find its percent composition means that we are to find to find the percentage of each of the constituents of the compound present.
The molar mass of monosodium glutamate is 169.11 gmol-1
Hence;
Percent of sodium= 23 gmol-1/169.11 gmol-1 × 100 = 13.6 % sodium
Percent of Carbon= 60 gmol-1/169.11 gmol-1 ×100 = 35.5 % carbon
Percent of hydrogen= 8/169.11 gmol-1 ×100 = 4.7% hydrogen
Percent nitrogen = 14/169.11 gmol-1 × 100 = 8.3% nitrogen
Percent oxygen = 64/169.11 gmol-1 ×100 = 37.8 % oxygen
Answer:
Explanation:
1. First take the cylinder volume formula:
2. Then take the values for the radius and the height of the cylinder and replace them into the formula:
3. Solve the equation:
Answer:
The protein has 4 subunits: 2 subunits of 90 kDa, 1 subunit of 160 kDa and 1 subunit of 60 kDa
Explanation:
In gel electrophoresis, the SDS agent produces denaturation of the protein and confers negative charge, so the protein subunits can migrate according to their masses. It produces dissociation of the protein in its subunits but it cannot disrupt disulphyde bridges (S-S) that can bond subunits together.
From the data, with SDS we observe 3 bands ⇒ 180 kDa + 160 kDa + 60 kDa
The addition of dithiotreitol (DTT), a reducing agent, produces the disruption of disulphyde bridges. From the data:
With DTT ⇒ 160 kDa + 90 kDa + 60 kDa
We observe that 160 kDa and 60 kDa subunits are conserved (they are the same as with SDS only), but 180 kDa subunit is missing and in its place appears a band of 90 kDa - a half 180 kDa.
So, the band at 180 kDa is composed by two subunits bonded by a disulphyde bridge.
Therefore, the composition of the protein is: <em>1 subunit of 160 kDa, 2 subunits of 90 kDa and 1 subunit of 60 kDa</em>.
