Answer:
See explaination
Explanation:
The Cys3-cys97 and cys21-cys142 disulfides restrict the unfolded state of lysozyme enzyme to a class of more compact structures with a less exposed hydrophobic surface, compared to the unfolded states of reduced/non-crosslinked lysozyme. there are 2 major factors which lead to the stabilization of lysozyme due to disulfide bonds-
1- increase in the loop size due to the formation of disulfide bonds that leads to an increase in the even entropic effect.
2- the region formed should be flexible. the strain energy due to the formation of the disulfide bond is lower.
cys21-cys142 has a higher Tm than the cys3-cys97 because it involves flexible parts of the molecule. 21 and 142 residues are located on opposite sides of the active-site cleft where significant hinge-bending motion is seen. this introduces minimal strain in the protein.
You must use 1880 mL of O₂ to react with 4.03 g Mg.
A_r: 24.305
2Mg + O₂ ⟶ 2MgO
<em>Moles of Mg</em> = 4.03 g Mg × (1 mol Mg/24.305 g Mg) = 0.1658 mol Mg
<em>Moles of O₂</em> = 0.1658 mol Mg × (1 mol O₂/2 mol Mg) = 0.082 90 mol O₂
STP is 25 °C and 1 bar. At STP, 1 mol of an ideal gas has a volume of <em>22.71 L</em>.
<em>Volume of O₂</em> = 0.082 90 mol O₂ × (22.71 L O₂/1 mol O₂) = 1.88 L = 1880 mL
A because cation is positive and anion is negative evening it out at constant.
