Answer:
In the unfolded polypeptide, there are ordered solvation shells of water around the protein
groups. The number of water molecules involved in such ordered shells is reduced when the protein
folds, resulting in higher entropy. Hence, the lower free energy of the native conformation.
Explanation:
Answer: Please See answers below
Explanation:
A. Ions in mobile phase are attracted to counterions covalently attached to stationary phase -----Ion Exchange Chromatography
B. Solute in mobile phase is attracted to specific groups covalently attached to stationary phase -----Affinity Chromatography
C. Solute equilibrates between mobile phase and surface of stationary phase -----Adsorption Chromatography
D. Solute equilibrates between mobile phase and film of liquid attached to stationary phase --- Partition Chromatography
E. Different-sized solutes penetrate pores in stationary phase to different extents. Large solutes are eluted first.
---Molecular Exclusion Chromatography
Answer:
i would say
112 degrees Fahrenheit
or
100 degrees celsius
Explanation:
brainliest pls if correct
The solution would be like this for this specific problem:
<span><span>Given:
</span>moles of Fe = 31.0 g</span>
So first, we get the molar mass of Fe2O3:
<span>The molar mass of Fe2O3 = 2 x Fe (2 x 55.85) + 3 x O (3 x
16.00) = 159.7 g/mole. <span>
27.4.0 g Fe2O3 x (1 mole Fe2O3 / 159.7 g Fe2O3) = 0.172moles of
Fe2O3
In the formula Fe2O3, there are 2 Fe. So, 1 mole of the
compound Fe2O3 is composed of 2 moles of Fe.
<span>0.172 moles of Fe2O3 x (2 mole Fe / 1 mole Fe2O3) = 0.344
moles of Fe
Therefore, there are 0.344 moles </span></span><span>of fe that are present in 27.4 g of the
compound.</span></span>