Chapter 4 Solid-State NMR Studies of Collagen Structure and Dynamics in Isolated Fibrils and in Biological Tissues

作者: Daniel Huster

DOI: 10.1016/S0066-4103(08)00004-5

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摘要: Collagen is the most abundant protein on earth. Having a unique amino acid sequence featuring high content of glycine, proline and hydroxyproline residues, collagen α-chains form slightly twisted left-handed polyproline-II-type helix with three acids per turn. Three such triple helix, which basic building block for fibrils that are characterized by very tensile strength. structures extracellular matrix many biological tissues as bone, skin, cartilage, teeth, blood vessels tendon others. Since neither water soluble nor does it highly ordered crystals, significant amount information about isolated tissue has been acquired solid-state NMR techniques over last 30 years. This review will provide an overview applications to study structural dynamical features collagen. The discussed examples include static magic-angle spinning studies well dynamics in cartilage bone. Finally, interaction be molecular basis magnetic resonance imaging orientation tissues.

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