| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-128 |
Sentence |
denotes |
Characterization by NMR and molecular modeling of the binding of polyisoprenols and polyisoprenyl recognition sequence peptides: |
| T1 |
0-128 |
Sentence |
denotes |
Characterization by NMR and molecular modeling of the binding of polyisoprenols and polyisoprenyl recognition sequence peptides: |
| T1 |
0-128 |
Sentence |
denotes |
Characterization by NMR and molecular modeling of the binding of polyisoprenols and polyisoprenyl recognition sequence peptides: |
| TextSentencer_T2 |
129-198 |
Sentence |
denotes |
3D structure of the complexes reveals sites of specific interactions. |
| T2 |
129-198 |
Sentence |
denotes |
3D structure of the complexes reveals sites of specific interactions. |
| T2 |
129-198 |
Sentence |
denotes |
3D structure of the complexes reveals sites of specific interactions. |
| TextSentencer_T3 |
199-498 |
Sentence |
denotes |
The objective of these studies was to test the hypothesis that proteins that contain potential polyisoprenyl recognition sequences (PIRSs) in their transmembrane-spanning domain can bind to the polyisoprenyl (PI) glycosyl carrier lipids undecaprenyl phosphate (C55-P) and dolichyl phosphate (C95-P). |
| T3 |
199-498 |
Sentence |
denotes |
The objective of these studies was to test the hypothesis that proteins that contain potential polyisoprenyl recognition sequences (PIRSs) in their transmembrane-spanning domain can bind to the polyisoprenyl (PI) glycosyl carrier lipids undecaprenyl phosphate (C55-P) and dolichyl phosphate (C95-P). |
| T3 |
199-498 |
Sentence |
denotes |
The objective of these studies was to test the hypothesis that proteins that contain potential polyisoprenyl recognition sequences (PIRSs) in their transmembrane-spanning domain can bind to the polyisoprenyl (PI) glycosyl carrier lipids undecaprenyl phosphate (C55-P) and dolichyl phosphate (C95-P). |
| TextSentencer_T4 |
499-656 |
Sentence |
denotes |
A number of prokaryotic and eukaryotic glycosyltransferases that utilize PI coenzymes contain a conserved PIRS postulated to be the active PI binding domain. |
| T4 |
499-656 |
Sentence |
denotes |
A number of prokaryotic and eukaryotic glycosyltransferases that utilize PI coenzymes contain a conserved PIRS postulated to be the active PI binding domain. |
| T4 |
499-656 |
Sentence |
denotes |
A number of prokaryotic and eukaryotic glycosyltransferases that utilize PI coenzymes contain a conserved PIRS postulated to be the active PI binding domain. |
| TextSentencer_T5 |
657-809 |
Sentence |
denotes |
To study this problem, we first determined the 3D structure of a PIRS peptide, NeuE, by homonuclear 2D 1H-nuclear magnetic resonance (NMR) spectroscopy. |
| T5 |
657-809 |
Sentence |
denotes |
To study this problem, we first determined the 3D structure of a PIRS peptide, NeuE, by homonuclear 2D 1H-nuclear magnetic resonance (NMR) spectroscopy. |
| T5 |
657-809 |
Sentence |
denotes |
To study this problem, we first determined the 3D structure of a PIRS peptide, NeuE, by homonuclear 2D 1H-nuclear magnetic resonance (NMR) spectroscopy. |
| TextSentencer_T6 |
810-1043 |
Sentence |
denotes |
Experimentally generated distance constraints derived from nuclear Overhauser enhancement and torsion angle constraints derived from coupling constants were used for restrained molecular dynamics and energy minimization calculations. |
| T6 |
810-1043 |
Sentence |
denotes |
Experimentally generated distance constraints derived from nuclear Overhauser enhancement and torsion angle constraints derived from coupling constants were used for restrained molecular dynamics and energy minimization calculations. |
| T6 |
810-1043 |
Sentence |
denotes |
Experimentally generated distance constraints derived from nuclear Overhauser enhancement and torsion angle constraints derived from coupling constants were used for restrained molecular dynamics and energy minimization calculations. |
| TextSentencer_T7 |
1044-1171 |
Sentence |
denotes |
Molecular models of the NeuE peptide were built based on calculations of energy minimization using the DGII program NMRchitect. |
| T7 |
1044-1171 |
Sentence |
denotes |
Molecular models of the NeuE peptide were built based on calculations of energy minimization using the DGII program NMRchitect. |
| T7 |
1044-1171 |
Sentence |
denotes |
Molecular models of the NeuE peptide were built based on calculations of energy minimization using the DGII program NMRchitect. |
| TextSentencer_T8 |
1172-1437 |
Sentence |
denotes |
3D models of dolichol (C95) and C95-P were built based on our 2D 1H-NMR nuclear Overhauser enhancement spectroscopy (NOESY) results and refined by energy minimization with respect to all atoms using the AMBER (assisted modeling with energy refinements) force field. |
| T8 |
1172-1437 |
Sentence |
denotes |
3D models of dolichol (C95) and C95-P were built based on our 2D 1H-NMR nuclear Overhauser enhancement spectroscopy (NOESY) results and refined by energy minimization with respect to all atoms using the AMBER (assisted modeling with energy refinements) force field. |
| T8 |
1172-1437 |
Sentence |
denotes |
3D models of dolichol (C95) and C95-P were built based on our 2D 1H-NMR nuclear Overhauser enhancement spectroscopy (NOESY) results and refined by energy minimization with respect to all atoms using the AMBER (assisted modeling with energy refinements) force field. |
| TextSentencer_T9 |
1438-1619 |
Sentence |
denotes |
Our energy minimization studies were carried out on a conformational model of dolichol that was originally derived from small-angle X-ray scattering and molecular mechanics methods. |
| T9 |
1438-1619 |
Sentence |
denotes |
Our energy minimization studies were carried out on a conformational model of dolichol that was originally derived from small-angle X-ray scattering and molecular mechanics methods. |
| T9 |
1438-1619 |
Sentence |
denotes |
Our energy minimization studies were carried out on a conformational model of dolichol that was originally derived from small-angle X-ray scattering and molecular mechanics methods. |
| TextSentencer_T10 |
1620-1781 |
Sentence |
denotes |
These results revealed that the PIs are conformationally nearly identical tripartite molecules, with their three domains arranged in a coiled, helical structure. |
| T10 |
1620-1781 |
Sentence |
denotes |
These results revealed that the PIs are conformationally nearly identical tripartite molecules, with their three domains arranged in a coiled, helical structure. |
| T10 |
1620-1781 |
Sentence |
denotes |
These results revealed that the PIs are conformationally nearly identical tripartite molecules, with their three domains arranged in a coiled, helical structure. |
| TextSentencer_T11 |
1782-2050 |
Sentence |
denotes |
Analyses of the intermolecular cross-peaks in the 2D NOESY spectra of PIRS peptides in the presence of PIs confirmed a highly specific interaction and identified key contact amino acids in the NeuE peptide that constituted a binding motif for interacting with the PIs. |
| T11 |
1782-2050 |
Sentence |
denotes |
Analyses of the intermolecular cross-peaks in the 2D NOESY spectra of PIRS peptides in the presence of PIs confirmed a highly specific interaction and identified key contact amino acids in the NeuE peptide that constituted a binding motif for interacting with the PIs. |
| T11 |
1782-2050 |
Sentence |
denotes |
Analyses of the intermolecular cross-peaks in the 2D NOESY spectra of PIRS peptides in the presence of PIs confirmed a highly specific interaction and identified key contact amino acids in the NeuE peptide that constituted a binding motif for interacting with the PIs. |
| TextSentencer_T12 |
2051-2176 |
Sentence |
denotes |
These studies also showed that subtle conformational changes occurred within both the PIs and the NeuE peptide after binding. |
| T12 |
2051-2176 |
Sentence |
denotes |
These studies also showed that subtle conformational changes occurred within both the PIs and the NeuE peptide after binding. |
| T12 |
2051-2176 |
Sentence |
denotes |
These studies also showed that subtle conformational changes occurred within both the PIs and the NeuE peptide after binding. |
| TextSentencer_T13 |
2177-2288 |
Sentence |
denotes |
3D structures of the resulting molecular complexes revealed that each PI could bind more than one PIRS peptide. |
| T13 |
2177-2288 |
Sentence |
denotes |
3D structures of the resulting molecular complexes revealed that each PI could bind more than one PIRS peptide. |
| T13 |
2177-2288 |
Sentence |
denotes |
3D structures of the resulting molecular complexes revealed that each PI could bind more than one PIRS peptide. |
| TextSentencer_T14 |
2289-2504 |
Sentence |
denotes |
These studies thus represent the first evidence for a direct physical interaction between specific contact amino acids in the PIRS peptides and the PIs and supports the hypothesis of a bifunctional role for the PIs. |
| T14 |
2289-2504 |
Sentence |
denotes |
These studies thus represent the first evidence for a direct physical interaction between specific contact amino acids in the PIRS peptides and the PIs and supports the hypothesis of a bifunctional role for the PIs. |
| T14 |
2289-2504 |
Sentence |
denotes |
These studies thus represent the first evidence for a direct physical interaction between specific contact amino acids in the PIRS peptides and the PIs and supports the hypothesis of a bifunctional role for the PIs. |
| TextSentencer_T15 |
2505-2759 |
Sentence |
denotes |
The central idea is that these superlipids may serve as a structural scaffold to organize and stabilize in functional domains PIRS-containing proteins within multiglycosyltransferase complexes that participate in biosynthetic and translocation processes. |
| T15 |
2505-2759 |
Sentence |
denotes |
The central idea is that these superlipids may serve as a structural scaffold to organize and stabilize in functional domains PIRS-containing proteins within multiglycosyltransferase complexes that participate in biosynthetic and translocation processes. |
| T15 |
2505-2759 |
Sentence |
denotes |
The central idea is that these superlipids may serve as a structural scaffold to organize and stabilize in functional domains PIRS-containing proteins within multiglycosyltransferase complexes that participate in biosynthetic and translocation processes. |