Harm van Ruremonde
Collagen is the most abundant protein in mammals and can be found in several tissues including bone. The collagen molecules consist of three α-chains which are folded into a triple helix. During the assembly of the collagen molecule the chains undergo several post-translational modifications, which are crucial for the formation of inter-molecular cross-links. The cross-link density of collagen differs per species and tissue. How the molecular structure and cross-link density of collagen are involved in the mineralization of bone fascinates me. To understand the relation between the molecular structure and the mineralization of collagen electron microscopy will be combined with Secondary Ions Mass Spectrometry (SIMS). This allows spatial-resolved chemical and structural analysis of 3D structures to correlate organic and inorganic components during collagen mineralization.
Harm van Ruremonde is a doctoral candidate at the laboratory of Materials and Interface Chemistry. He received his bachelor’s degree in Chemistry at the Fontys University of Applied Sciences and his master’s degree in Molecular Systems and Materials Chemistry at the Eindhoven University of Technology. During his graduation project under the supervision of Prof. Nico Sommerdijk, Harm focused on the evaluation of bone biosynthesis in a living in vitro system using cryo electron microscopy. Since July 2018 Harm continues his research on bone formation and is now focusing on the molecular structure of collagen and how this influences the biomineralization of bone.
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