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What does glycosylation affect in proteins?

Their energy production capability

Protein stability, recognition, and folding

Glycosylation is a crucial post-translational modification in which carbohydrate molecules are attached to proteins. This process significantly influences several aspects of protein behavior and characteristics, primarily enhancing their stability, facilitating proper folding, and playing a vital role in cellular recognition processes.

Firstly, glycosylation can stabilize proteins by protecting them from proteolytic degradation, thereby extending their half-life in the extracellular environment. The attached sugar moieties can also influence the three-dimensional structure of the protein, assisting in achieving and maintaining its proper folding. This correct folding is essential for a protein's functionality.

Moreover, glycosylation plays a pivotal role in cellular recognition. The carbohydrate chains added to proteins can serve as recognition sites for various receptors, enabling interactions between cells, and between cells and extracellular matrices, which are crucial for many biological processes, including immune responses and cellular signaling.

In contrast, the other options focus on aspects such as energy production, secretion speed, and degradation processes, which are not directly altered by glycosylation. For instance, while glycans contribute to intracellular processes and overall protein lifecycle, the primary effects of glycosylation are more aligned with stability, recognition, and proper folding of the proteins, establishing the selected response as the

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The speed of their secretion from the cell

Their degradation process in lysosomes

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