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They form long protein filaments, rod- or wire-like shapes. They are usually inert structural or storage proteins. They are generally water-insoluble and are found as an aggregate due to hydrophobic R groups that stick out of the molecule. The amino acid sequences they are made from often have limited residues with repeats. These can form unusual secondary structures, e.g. collagen triple helix. The structures often contain 'cross-links' between chains, for example cys-cys disulfide bonds between keratin chains.
Globular proteins tend to denature more easily than fibrous proteins.
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Fibrous proteins also gain strength due to interactions between the side chains of the residues. The alpha-keratin polypeptides , for example, have a large number of cystine residues, which can form disulfide bonds .
Coils such as those found in alpha-keratin are not the only structural motifs present in fibrous proteins. Silk, for example, is largely composed of fibrous proteins whose structures resemble interleaved sheets.
Coils such as those found in alpha-keratin are not the only structural motifs present in fibrous proteins. Silk, for example, is largely composed of fibrous proteins whose structures resemble interleaved sheets.
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