A great review article, written by our own Dr. Mike Kirkness, discussing the structural stability of the collagen triple helix was just published in Current Opinion in Chemical Biology. This article discusses the challenges associated with probing and understanding the mechanical properties of the collagen triple helix by modeling it as a semiflexible rod. He explains the shortcomings of current techniques and gives insight into new theories about what properties influence the complex mechanical stability of the collagen triple helix. Great work Mike!

Abstract: The primary building block of the body is collagen, which is found in the extracellular matrix and in many stress-bearing tissues such as tendon and cartilage. It provides elasticity and support to cells and tissues while influencing biological pathways including cell signaling, motility, and differentiation. Collagen’s unique triple helical structure is thought to impart mechanical stability. However, detailed experimental studies on its molecular mechanics have been only recently emerging. Here, we review the treatment of the triple helix as a homogeneous flexible rod, including bend (standard worm-like chain model), twist, and stretch deformations, and the assumption of backbone linearity. Additionally, we discuss protein-specific properties of the triple helix including sequence dependence, and relate single-molecule mechanics to collagen’s physiological context.


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