| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-127 |
Sentence |
denotes |
Structural basis for carbohydrate-binding specificity--a comparative assessment of two engineered carbohydrate-binding modules. |
| T1 |
0-127 |
Sentence |
denotes |
Structural basis for carbohydrate-binding specificity--a comparative assessment of two engineered carbohydrate-binding modules. |
| T1 |
0-127 |
Sentence |
denotes |
Structural basis for carbohydrate-binding specificity--a comparative assessment of two engineered carbohydrate-binding modules. |
| TextSentencer_T2 |
128-280 |
Sentence |
denotes |
Detection, immobilization and purification of carbohydrates can be done using molecular probes that specifically bind to targeted carbohydrate epitopes. |
| T2 |
128-280 |
Sentence |
denotes |
Detection, immobilization and purification of carbohydrates can be done using molecular probes that specifically bind to targeted carbohydrate epitopes. |
| T2 |
128-280 |
Sentence |
denotes |
Detection, immobilization and purification of carbohydrates can be done using molecular probes that specifically bind to targeted carbohydrate epitopes. |
| TextSentencer_T3 |
281-453 |
Sentence |
denotes |
Carbohydrate-binding modules (CBMs) are discrete parts of carbohydrate-hydrolyzing enzymes that can be engineered to bind and detect specifically a number of carbohydrates. |
| T3 |
281-453 |
Sentence |
denotes |
Carbohydrate-binding modules (CBMs) are discrete parts of carbohydrate-hydrolyzing enzymes that can be engineered to bind and detect specifically a number of carbohydrates. |
| T3 |
281-453 |
Sentence |
denotes |
Carbohydrate-binding modules (CBMs) are discrete parts of carbohydrate-hydrolyzing enzymes that can be engineered to bind and detect specifically a number of carbohydrates. |
| TextSentencer_T4 |
454-627 |
Sentence |
denotes |
Design and engineering of CBMs have benefited greatly from structural studies that have helped us to decipher the basis for specificity in carbohydrate-protein interactions. |
| T4 |
454-627 |
Sentence |
denotes |
Design and engineering of CBMs have benefited greatly from structural studies that have helped us to decipher the basis for specificity in carbohydrate-protein interactions. |
| T4 |
454-627 |
Sentence |
denotes |
Design and engineering of CBMs have benefited greatly from structural studies that have helped us to decipher the basis for specificity in carbohydrate-protein interactions. |
| TextSentencer_T5 |
628-761 |
Sentence |
denotes |
However, more studies are needed to predict which modifications in a CBM would generate probes with predetermined binding properties. |
| T5 |
628-761 |
Sentence |
denotes |
However, more studies are needed to predict which modifications in a CBM would generate probes with predetermined binding properties. |
| T5 |
628-761 |
Sentence |
denotes |
However, more studies are needed to predict which modifications in a CBM would generate probes with predetermined binding properties. |
| TextSentencer_T6 |
762-1018 |
Sentence |
denotes |
In this report, we present the crystal structures of two highly related engineered CBMs with different binding specificity profiles: X-2, which is specific for xylans and the L110F mutant of X-2, which binds xyloglucans and β-glucans in addition to xylans. |
| T6 |
762-1018 |
Sentence |
denotes |
In this report, we present the crystal structures of two highly related engineered CBMs with different binding specificity profiles: X-2, which is specific for xylans and the L110F mutant of X-2, which binds xyloglucans and β-glucans in addition to xylans. |
| T6 |
762-1018 |
Sentence |
denotes |
In this report, we present the crystal structures of two highly related engineered CBMs with different binding specificity profiles: X-2, which is specific for xylans and the L110F mutant of X-2, which binds xyloglucans and β-glucans in addition to xylans. |
| TextSentencer_T7 |
1019-1186 |
Sentence |
denotes |
The structures of the modules were solved both in the apo form and complexed with oligomers of xylose, as well as with an oligomer of glucose in the case of X-2 L110F. |
| T7 |
1019-1186 |
Sentence |
denotes |
The structures of the modules were solved both in the apo form and complexed with oligomers of xylose, as well as with an oligomer of glucose in the case of X-2 L110F. |
| T7 |
1019-1186 |
Sentence |
denotes |
The structures of the modules were solved both in the apo form and complexed with oligomers of xylose, as well as with an oligomer of glucose in the case of X-2 L110F. |
| TextSentencer_T8 |
1187-1383 |
Sentence |
denotes |
The mutation, leucine to phenylalanine, converting the specific module into a cross-reactive one, introduces a crucial hydrogen-π interaction that allows the mutant to retain glucan-based ligands. |
| T8 |
1187-1383 |
Sentence |
denotes |
The mutation, leucine to phenylalanine, converting the specific module into a cross-reactive one, introduces a crucial hydrogen-π interaction that allows the mutant to retain glucan-based ligands. |
| T8 |
1187-1383 |
Sentence |
denotes |
The mutation, leucine to phenylalanine, converting the specific module into a cross-reactive one, introduces a crucial hydrogen-π interaction that allows the mutant to retain glucan-based ligands. |
| TextSentencer_T9 |
1384-1619 |
Sentence |
denotes |
The cross-reactivity of X-2 L110F is furthermore made possible by the plasticity of the protein, in particular, of residue R142, which permits accommodation of an extra hydroxymethyl group present in cellopentaose and not xylopentaose. |
| T9 |
1384-1619 |
Sentence |
denotes |
The cross-reactivity of X-2 L110F is furthermore made possible by the plasticity of the protein, in particular, of residue R142, which permits accommodation of an extra hydroxymethyl group present in cellopentaose and not xylopentaose. |
| T9 |
1384-1619 |
Sentence |
denotes |
The cross-reactivity of X-2 L110F is furthermore made possible by the plasticity of the protein, in particular, of residue R142, which permits accommodation of an extra hydroxymethyl group present in cellopentaose and not xylopentaose. |
| TextSentencer_T10 |
1620-1832 |
Sentence |
denotes |
Altogether, this study shows, in structural detail, altered protein-carbohydrate interactions that have high impact on the binding properties of a carbohydrate probe but are introduced through simple mutagenesis. |
| T10 |
1620-1832 |
Sentence |
denotes |
Altogether, this study shows, in structural detail, altered protein-carbohydrate interactions that have high impact on the binding properties of a carbohydrate probe but are introduced through simple mutagenesis. |
| T10 |
1620-1832 |
Sentence |
denotes |
Altogether, this study shows, in structural detail, altered protein-carbohydrate interactions that have high impact on the binding properties of a carbohydrate probe but are introduced through simple mutagenesis. |