Fibrous proteins have a fiber-like structure with parallel polypeptide chains held together by hydrogen and disulphide bonds. Examples include keratin (in hair, wool, silk) and myosin (in muscles).
How are fibrous proteins characterized in terms of molecular shape, and what bonds hold their polypeptide chains together?
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Fibrous proteins are characterized by an elongated, thread-like molecular shape with repeating structural motifs. Their polypeptide chains are typically arranged in parallel or anti-parallel fashion, forming long fibers or sheets. The secondary structures, like α-helices or β-sheets, predominate in fibrous proteins. These proteins are held together by strong and stable bonds, including hydrogen bonds and disulfide bridges. The repetitive and regular structures contribute to the overall stability and resilience of fibrous proteins, making them well-suited for structural roles, such as providing support and strength in tissues like collagen and keratin.