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1
Q30940504-271EDF2D-E949-4B7E-AA8E-F5F4936247DF
Q30940504-271EDF2D-E949-4B7E-AA8E-F5F4936247DF
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http://www.wikidata.org/entity/statement/Q30940504-271EDF2D-E949-4B7E-AA8E-F5F4936247DF
Hydroxylation-induced stabilization of the collagen triple helix. Acetyl-(glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)(10)-NH(2) forms a highly stable triple helix.
P2860
Q30940504-271EDF2D-E949-4B7E-AA8E-F5F4936247DF
BestRank
Statement
http://www.wikidata.org/entity/statement/Q30940504-271EDF2D-E949-4B7E-AA8E-F5F4936247DF
rank
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wasDerivedFrom
69edc4ae22bc7d88b6e1418d5ffd094d6d661f2f
P2860
Structure formation in the C terminus of type III collagen guides disulfide cross-linking.