1992
DOI: 10.1016/0022-2836(92)90878-n
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Unique side-chain conformation encoding for chirality and azimuthal orientation in the molecular packing of skin collagen

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Cited by 34 publications
(27 citation statements)
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“…Several recent studies addressing molecular packing of collagen are pertinent to this question. Katz and David [19] conducted a detailed analysis of molecular packing in type I collagen from skin, in which they identified specific regions encoding for chirality and orientation, both of which have been reported to affect second harmonic intensity. Specifically, they identified a sequence of three amino acids that, when present in all three chains, leads to a conformational change that increases molecular helicity.…”
Section: Discussionmentioning
confidence: 99%
“…Several recent studies addressing molecular packing of collagen are pertinent to this question. Katz and David [19] conducted a detailed analysis of molecular packing in type I collagen from skin, in which they identified specific regions encoding for chirality and orientation, both of which have been reported to affect second harmonic intensity. Specifically, they identified a sequence of three amino acids that, when present in all three chains, leads to a conformational change that increases molecular helicity.…”
Section: Discussionmentioning
confidence: 99%
“…29 This nonequivalent environment of the same residue in the three chains may have implications for the association of collagen molecules into larger aggregates in their functional state or the specific binding sites of collagens. A possible consequence of this inequivalence might be a nonsymmetric character of the collagen triple helix, 38 which could give rise to non symmetric supermolecular aggregates.…”
Section: Figurementioning
confidence: 99%
“…Moreover, the dipoles of water molecules contribute to the polar nature of collagen [23], as they exist in a hydrated state during the process of wet bonding. Molecular modeling of collagen with adjacent charged residues predicted that side-chains participate in the formation of intra-chain and inter-helix ion pairs [24,25]. Moreover, proteoglycans associated with dentin collagen fibrils are characterized by lateral glycosaminoglycans chains with negatively charged residues that are responsible for the high water binding and tissue swelling behavior of this collagen-proteoglycan complex [26,27].…”
Section: Fig 2 -Fe-sem Micrographs Of Bonded Interfaces In Single Bomentioning
confidence: 99%