| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-70 |
Sentence |
denotes |
Interaction of prolyl 4-hydroxylase with synthetic peptide substrates. |
| T2 |
71-129 |
Sentence |
denotes |
A conformational model for collagen proline hydroxylation. |
| T3 |
130-393 |
Sentence |
denotes |
With the aim of understanding the structural basis for the substrate specificity of collagen prolyl 4-hydroxylase, we have studied the conformational features of synthetic oligopeptide substrates and their interaction with the enzyme purified from chicken embryo. |
| T4 |
394-871 |
Sentence |
denotes |
Circular dichroism and infrared spectral data, taken in conjunction with relevant crystal structure data, indicated an equilibrium mixture of the polyproline-II (PP-II) helix, the beta-turn, and the random coil conformations in aqueous and trifluoroethanol solutions of the "collagen-related" peptides: t-Boc-Pro-Pro-Gly-Pro-OH, t-Boc-Pro-Pro-Gly-Pro-NHCH3, t-Pro-Pro-Gly-Pro-Pro-OH, t-Boc-Pro-Pro-Ala-Pro-OH, and t-Boc-Pro-Pro-Gln-Pro-OCH3, where t-Boc is tert-butoxycarbonyl. |
| T5 |
872-1084 |
Sentence |
denotes |
In another set of peptides related to elastin, t-Boc-Val-Pro-Gly-Val-OH and t-Boc-Gly-Val-Pro-Gly-Val-OH, the data indicated the beta-structure, rather than the PP-II helix, was in equilibrium with the beta-turn. |
| T6 |
1085-1302 |
Sentence |
denotes |
Kinetic parameters for the enzymatic hydroxylation of the peptides showed that as a group, the first (proline-rich) set of peptides has higher Km values and lower Vmax and Kcat/Km values than the valine-rich peptides. |
| T7 |
1303-1461 |
Sentence |
denotes |
Data on the inhibition of hydroxylation of the standard assay substrate (Pro-Pro-Gly)10 by the oligopeptides pointed to common binding sites for the peptides. |
| T8 |
1462-1601 |
Sentence |
denotes |
Hydroxyproline-containing peptides had no effect on the hydroxylation of the standard substrate, showing the absence of product inhibition. |
| T9 |
1602-1832 |
Sentence |
denotes |
Based on these and earlier data, we propose that in collagen and related peptides, a supersecondary structure consisting of the PP-II helix followed by the beta-turn is the minimal structural requirement for proline hydroxylation. |
| T10 |
1833-1995 |
Sentence |
denotes |
The PP-II structure would aid effective interaction at the substrate binding subsites, while the beta-turn would be essential at the catalytic site of the enzyme. |
| T11 |
1996-2103 |
Sentence |
denotes |
In elastin and related peptides, the beta-strand structure may be interchangeable with the PP-II structure. |
| T12 |
2104-2257 |
Sentence |
denotes |
This conformational model for proline hydroxylation resolves the discrepancies in earlier proposals on the substrate specificity of prolyl 4-hydroxylase. |
| T13 |
2258-2353 |
Sentence |
denotes |
It is also consistent with the available information on the active site geometry of the enzyme. |
| T1 |
0-70 |
Sentence |
denotes |
Interaction of prolyl 4-hydroxylase with synthetic peptide substrates. |
| T2 |
71-129 |
Sentence |
denotes |
A conformational model for collagen proline hydroxylation. |
| T3 |
130-393 |
Sentence |
denotes |
With the aim of understanding the structural basis for the substrate specificity of collagen prolyl 4-hydroxylase, we have studied the conformational features of synthetic oligopeptide substrates and their interaction with the enzyme purified from chicken embryo. |
| T4 |
394-871 |
Sentence |
denotes |
Circular dichroism and infrared spectral data, taken in conjunction with relevant crystal structure data, indicated an equilibrium mixture of the polyproline-II (PP-II) helix, the beta-turn, and the random coil conformations in aqueous and trifluoroethanol solutions of the "collagen-related" peptides: t-Boc-Pro-Pro-Gly-Pro-OH, t-Boc-Pro-Pro-Gly-Pro-NHCH3, t-Pro-Pro-Gly-Pro-Pro-OH, t-Boc-Pro-Pro-Ala-Pro-OH, and t-Boc-Pro-Pro-Gln-Pro-OCH3, where t-Boc is tert-butoxycarbonyl. |
| T5 |
872-1084 |
Sentence |
denotes |
In another set of peptides related to elastin, t-Boc-Val-Pro-Gly-Val-OH and t-Boc-Gly-Val-Pro-Gly-Val-OH, the data indicated the beta-structure, rather than the PP-II helix, was in equilibrium with the beta-turn. |
| T6 |
1085-1302 |
Sentence |
denotes |
Kinetic parameters for the enzymatic hydroxylation of the peptides showed that as a group, the first (proline-rich) set of peptides has higher Km values and lower Vmax and Kcat/Km values than the valine-rich peptides. |
| T7 |
1303-1461 |
Sentence |
denotes |
Data on the inhibition of hydroxylation of the standard assay substrate (Pro-Pro-Gly)10 by the oligopeptides pointed to common binding sites for the peptides. |
| T8 |
1462-1601 |
Sentence |
denotes |
Hydroxyproline-containing peptides had no effect on the hydroxylation of the standard substrate, showing the absence of product inhibition. |
| T9 |
1602-1832 |
Sentence |
denotes |
Based on these and earlier data, we propose that in collagen and related peptides, a supersecondary structure consisting of the PP-II helix followed by the beta-turn is the minimal structural requirement for proline hydroxylation. |
| T10 |
1833-1995 |
Sentence |
denotes |
The PP-II structure would aid effective interaction at the substrate binding subsites, while the beta-turn would be essential at the catalytic site of the enzyme. |
| T11 |
1996-2103 |
Sentence |
denotes |
In elastin and related peptides, the beta-strand structure may be interchangeable with the PP-II structure. |
| T12 |
2104-2257 |
Sentence |
denotes |
This conformational model for proline hydroxylation resolves the discrepancies in earlier proposals on the substrate specificity of prolyl 4-hydroxylase. |
| T13 |
2258-2353 |
Sentence |
denotes |
It is also consistent with the available information on the active site geometry of the enzyme. |
