Keywords: Collagen, Hydration, Hydroxyproline, Supermolecular Structure, Triple Helix, Glycine, Amino Acid Sequence, Article, Crystal Structure, Hydrogen Bond, Molecular Model, Priority Journal, Protein Assembly, Protein Conformation, Protein Structure, X Ray Crystallography, X-Ray, Oligopeptides, Repetitive Sequences, Nucleic Acid,
Affiliations: Department of Chemistry, Rutgers University, 610 Taylor Rd, Piscataway, NJ 08854-8087, United States
Waksman Institute, Piscataway, NJ 08855, United States
Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08855, United States
Ctro. di Stud. di Biocristallografia, CNR and Dipartimento di Chimica, Universita' di Napoli, via Mezzocannone 4, 80134 Napoli, Italy
Purdue University, Department of Biological Sciences, West Lafayette, IN 47907, United States
References: Not available.
X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly)
The crystal structure of the triple-helical peptide (Pro-Pro-Gly)10 has been re-determined to obtain a more accurate description for this widely studied collagen model and to provide a comparison with the recent high-resolution crystal structure of a collagen-like peptide containing Pro-Hyp-Gly regions. This structure demonstrated that hydroxyproline participates extensively in a repetitive hydrogen-bonded assembly between the peptide and the solvent molecules. Two separate structural studies of the peptide (Pro-Pro-Gly)10 were performed with different crystallization conditions, data collection temperatures, and X-ray sources. The polymer-like structure of one triple-helical repeat of Pro-Pro-Gly has been determined to 2.0 Å resolution in one case and 1.7 Å resolution in the other. The solvent structures of the two peptides were independently determined specifically for validation purposes. The two structures display a reverse chain trace compared with the original structure determination. In comparison with the Hyp-containing peptide, the two Pro-Pro-Gly structures demonstrate very similar molecular conformation and analogous hydration patterns involving carbonyl groups, but have different crystal packing. This difference in crystal packing indicates that the involvement of hydroxyproline in an extended hydration network is critical for the lateral assembly and supermolecular structure of collagen.
X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly)
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(462 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(531 views) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 ViewExport to BibTeXExport to EndNote