Fibrous proteins are generally

Fibrous proteins are characterized by their structural roles in the body, often providing strength and support. They typically have elongated, linear shapes, which contribute to their stability and resistance to unfolding or denaturation. This structural configuration allows fibrous proteins, such as collagen and keratin, to maintain their integrity under various conditions, including changes in heat and pH.

The resilience of fibrous proteins to environmental changes stems from their extensive network of intermolecular interactions, such as hydrogen bonds and disulfide bridges, which stabilize their overall structure. This stability is crucial for their functions, which often include providing tensile strength to tissues (in the case of collagen) or establishing protective barriers (as seen with keratin).

In contrast, globular proteins, which generally carry out more dynamic and complex functions, are often more sensitive to changes in their environment, leading them to denature under heat or varying pH levels. This distinction highlights why the correct answer emphasizes the robustness of fibrous proteins in the face of environmental changes.