When a protein is treated with a reducing agent such as 2-mercaptoethanol it becomes denatured. The interactions stabilizing the protein that are most affected and lead to denaturation with reducing agent treatment are

Disulfide linkage/bond

Explanation:

The tertiary and quarternary structure of the protein is stabilized by Disulfide linkage which is formed between two thiol groups in the protein. 2-mercaptoethanol is a reducing agent that breaks this disulfide bond.  

A protein becomes denature when it loses its native configuration and becomes inactive. So as 2-mercaptoethanol breaks disulfide bond in protein it looses its native configuration and becomes denatured. 2-mercaptoethanol  is used in SDS-PAGE to separate protein subunits. Therefore the correct answer is Disulfide linkage/bond.

132

explanation:

12

events in order:

1.       vishnu schist

2. zoroaster granite

3. bass limestone

4. hakatar   shale

5. igneous intrusion

6. shinumo quartzite

7. dox sandstone

8. tapeats limestone

9. bright angel shale

10. muav limestone

11. temple butte limestone

12. redwall limestone  

nonconformity

answer: the unkar group shows angular unconformity because the layers are turned at angle.

unconformity

answer: specifically the angular unconformity occurs between the cambrian and precambrian rocks. the dox sandstone, shinumo quartzite, hakatar shale, and bass limestone have been filled. an angular unconformity occurs between the cambrian and precambrian rocks. the dox sandstone, shinumo quartzite, hakatar shale, and bass limestone have been filled.

disconformity

answer: the disconformities aremarked irregular lines between the sedimentaryrocks layers.