Which type of protein is more sensitive to environmental changes?

Globular proteins are indeed more sensitive to environmental changes compared to other types of proteins. The structure of globular proteins is typically compact and tightly folded, allowing them to perform various functions such as catalysis, transport, and signaling. This unique three-dimensional structure is stabilized by a variety of interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions.

When there are changes in environmental conditions, such as temperature, pH, or ionic strength, these interactions can be disrupted. For example, an increase in temperature may cause the protein to denature, losing its functional shape and thus its ability to perform its biological role. This sensitivity to environmental factors is especially prominent in enzymes, which are a subset of globular proteins, as their activity is heavily reliant on maintaining their active site conformation.

In contrast, fibrous proteins, which usually have elongated, structural forms, tend to be more stable and resilient to changes in environmental conditions. They provide mechanical support and strength, often making them less sensitive to fluctuations in their surroundings. Structural proteins, such as collagen and keratin, are designed to maintain their shape and function even under stress.

Thus, the sensitivity of globular proteins to environmental changes is a key characteristic that differentiates them from other types,