Viruses always have a host to latch on. When latched on, viruses will inject its protein or RNA into the host.
Viruses aren’t considered organic.
Bacteria has a nucleus and cell membranes while viruses don’t
Viruses are not considered organic while bacteria are.
The differences are <u>the number of neutrons</u> and the <u>atomic mass</u><u /><u />.
Copper-63 has an atomic mass of 63 amu, and has 34 neutrons.
Copper-65 has an atomic mass of 65 amu, and has 36 neutrons.
Answer:
19.4%
Explanation:
Calcium Chlorate is Ca(ClO3)2
Now calculate the molar mass of Ca(ClO3)2
Ca = 40.1
Cl = 35.5
O = 16.0
But they are two chlorine atoms and six oxygen atoms. So you do this:
40.1 + 35.5(2) + 16.0(6) = 207.1 grams
Now find the molar mass of just calcium.
There is only one calcium atom.
So you do this.
40.1(1) = 40.1
Now divide the molar mass of calcium by the molar mass of calcium chlorate.
40.1 / 207.1 = 0.1936
0.1936 rounds to 0.194
Now multiply 0.194 * 100 and you will get 19.4
So the final answer is 19.4%.
Hope it helped!
Bonds formed between atoms can be classified as ionic and covalent
Ionic bonds are formed between atoms that have a high difference in the electronegativity values.
In contrast, bonds formed between atoms that have a difference in electronegativity lower than the ionic counterparts are polar covalent bonds. If the atoms have very similar electronegativities, they form non-polar covalent bonds.
In H2S, the S atom is bonded to 2 H atoms. The electronegativity of H = 2.2 and S= 2.56. Since the difference is not high the bond formed will be covalent (polar covalent).
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>.
