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High-resolution structures of collagen-like peptides [(Pro-Pro-Gly)4-Xaa-Yaa-Gly-(Pro-Pro-Gly)4]: Implications for triple-helix hydration and Hyp(X) puckering

✍ Scribed by Kenji Okuyama; Chizuru Hongo; Guanghan Wu; Kazunori Mizuno; Keiichi Noguchi; Shutoku Ebisuzaki; Yuji Tanaka; Norikazu Nishino; Hans Peter Bächinger

Publisher: Wiley (John Wiley & Sons)
Year: 2009
Tongue: English
Weight: 641 KB
Volume: 91
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.21138

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## Abstract Triple‐helical structures of (Pro‐Hyp‐Gly)n (__n__ = 10, 11) at 100 K and room temperature (RT) were analyzed at 1.26 Å resolution by using synchrotron radiation data. Totals of 49 and 42 water molecules per seven triplets in an asymmetric unit were found for the structures at 100 K and

Erratum: Crystal structures of collagen

Erratum: Crystal structures of collagen model peptides with Pro-Hyp-Gly repeating sequence at 1.26 Å resolution: Implications for proline ring puckering, Kenji Okuyama, Chizuru Hongo, Rie Fukushima, Guanghan Wu, Hirotaka Narita, Keiichi Noguchi, Yuji Tanaka, Norikazu Nishino, Biopolymers (Peptide Science)(2004)76(5) 367–377

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## Abstract The original article to which this Erratum refers was published in Biopolymers (Peptide Science) (2004) 76(5) 367–377