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Abstract:

Multicellular life is scaffolded by structures that maintain cells in the desired locations and organizations. The collagen family of proteins has been selected via evolution as the preferred building block of these extracellular structures, yet surprisingly, collagen proteins are structurally unstable at body temperature.

In this talk, I will introduce some of the fascinating physical properties of the unique triple-helix structure of collagen, and will highlight the results of our investigations into the sequence dependence of its mechanics and stability. Our single-molecule approaches include centrifuge force microscopy, optical tweezers and atomic force microscopy. Our work is revealing clues as to how stability is encoded within collagen鈥檚 sequence, and how collagen鈥檚 triple helix balances structural stability with responsiveness to applied force and chemical environment.

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