A molecular, morphometric and mechanical comparison of the structural elements of byssus from Mytilus edulis and Mytilus galloprovincialis
Jared M. Lucas*,
Eleonora Vaccaro and
J. Herbert Waite
Marine Science Institute and Molecular, Cellular and Developmental,
Biology Department, University of California at Santa Barbara, Santa Barbara,
CA 93106, USA

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Fig. 1. Protein sequence alignment between Mytilus edulis (upper) and
M. galloprovincialis (lower) precollagen D. Major domain structures
are boxed and indicated. Single amino acid substitutions are indicated by bold
italic type, and dashed lines indicate sequence deletions. Histidine residues
that may form metal chelate cross-links are in bold type. Breaks or kinks in
the collagen repeat structure are symbolized with a filled circle.
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Fig. 2. Protein sequence alignment between Mytilus edulis (upper) and
M. galloprovincialis (lower) precollagen NG. Major domain structures
are boxed and indicated. Single amino acid substitutions are indicated by bold
italic type, and dashed lines indicate sequence deletions. Histidine residues
that may form metal chelate cross-links are in bold type. Breaks or kinks in
the collagen repeat structure are symbolized with a filled circle.
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Fig. 3. Protein sequence alignment between Mytilus edulis (upper) and
M. galloprovincialis (lower) precollagen P. Major domain structures
are boxed and indicated. Single amino acid substitutions are indicated by bold
italic type, and dashed lines indicate sequence deletions. Histidine residues
that may form metal chelate cross-links are in bold type. Breaks or kinks in
the collagen repeat structure are symbolized with a filled circle.
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Fig. 5. Representative stress/strain curves for proximal, distal and whole threads
of Mytilus edulis (Me) and M. galloprovincialis (Mg).
Threads were pulled to breaking.
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© The Company of Biologists Ltd 2002