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<em>* Cell membrane</em>
<em>* Cytoplasm</em>
<em>* DNA and RNA</em>
<em>* Ribosome</em>
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500 mg in g :
1 g ----------- 1000 mg
? -------------- 500 mg
500 x 1 / 1000 => 0.5 g
total mass:
50 g + 0.5 g + 0.1 g => 50.6 g
hope this helps!
Answer:
A = shielding.
Explanation:
The addition of electron causes the atomic size increase from top to bottom due to increase in atomic number.
As the atomic number increased one more electron is added and because of this electron on more electronic shell is added. Thus the electron become more away from the nucleus as many of other electrons are present in the way from nucleus to the outer electrons.
The hold of nucleus becomes weaker. Although nuclear charge is also increased but at the same time other electrons shield the respective electrons. So effective nuclear charge is weaker than the actual nuclear charge.
Because of this shielding it is easy to remove the electrons or we can say ionization energy decreases.
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>.
