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The stability of the remarkable triple helix structure of collagen, the most abundant protein in mammalian organisms, has been investigated by tandem‐ion mobility and mass spectrometry. It was shown that collagen mimetic peptides can retain robust triple helix configurations in the absence of solvent. Moreover, the enhancement of the structural stability of the triple helix motifs through proline...
The origin of the triple‐helix structure and high stability of collagen has been debated for many years. As models of the triple helix and building blocks for new biomaterials, collagen mimetic peptide (CMP) assemblies have been deeply studied in the condensed phase. In particular, it was found that hydroxylation of proline, an abundant post‐translational modification in collagen, increases its stability...
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