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.

that would be called plucking : )

explanation:

''plucking, also referred to as quarrying, is a glacial phenomenon that is responsible for the erosion and transportation of individual pieces of bedrock, especially large "joint blocks". as a glacier moves down a valley, friction causes the basal ice of the glacier to melt and infiltrate joints (cracks) in the bedrock."