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. Author manuscript; available in PMC: 2007 Mar 29.
Published in final edited form as: Biochemistry. 2004 Jun 22;43(24):7653–7662. doi: 10.1021/bi049380h

Figure 3.

Figure 3

Proposed structure of the preCOLs making up the bulk of each mussel byssal thread. The block domain structure in 2D of a trimer is shown in panel A; the bent-core analogue of a trimer is shown in panel B; amino to carboxy terminal orientation is top-to-bottom. Summary of sequence features of each flank type and estimated stiffness constants (panel C) are as described in text. X represents any amino acid except glycine and alanine. Stiffness represents the initial modulus determined for fully hydrated biopolymers including the alanine-rich fibroin of Anaphe silk (14).