Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-51 |
Sentence |
denotes |
Proinsulin: a proposed three-dimensional structure. |
T2 |
52-169 |
Sentence |
denotes |
Empirical analysis of the primary structures of 10 mammalian C-peptides has indicated a conservation of conformation. |
T3 |
170-514 |
Sentence |
denotes |
The positioning of the C-peptide in the proinsulin molecule is essentially defined by the proposed secondary structure, the covalent connection to the A1 and B30 residues of insulin and the requirement that C-peptide lies against the exposed surface of the insulin hexamer, allowing a three-dimensional structure for proinsulin to be predicted. |
T4 |
515-685 |
Sentence |
denotes |
Conserved residues in the C-peptide are proximate to residues in insulin that are also conserved, suggesting that interactions between these residues are highly probable. |
T5 |
686-818 |
Sentence |
denotes |
Residues in insulin thought to be important for biological activity are principally those that interact with the C-peptide residues. |
T6 |
819-977 |
Sentence |
denotes |
The role of the C-peptide region in proinsulin in preventing expression of insulin activity and for nucleation of the folding of the prohormone are discussed. |
T1 |
0-51 |
Sentence |
denotes |
Proinsulin: a proposed three-dimensional structure. |
T2 |
52-169 |
Sentence |
denotes |
Empirical analysis of the primary structures of 10 mammalian C-peptides has indicated a conservation of conformation. |
T3 |
170-514 |
Sentence |
denotes |
The positioning of the C-peptide in the proinsulin molecule is essentially defined by the proposed secondary structure, the covalent connection to the A1 and B30 residues of insulin and the requirement that C-peptide lies against the exposed surface of the insulin hexamer, allowing a three-dimensional structure for proinsulin to be predicted. |
T4 |
515-685 |
Sentence |
denotes |
Conserved residues in the C-peptide are proximate to residues in insulin that are also conserved, suggesting that interactions between these residues are highly probable. |
T5 |
686-818 |
Sentence |
denotes |
Residues in insulin thought to be important for biological activity are principally those that interact with the C-peptide residues. |
T6 |
819-977 |
Sentence |
denotes |
The role of the C-peptide region in proinsulin in preventing expression of insulin activity and for nucleation of the folding of the prohormone are discussed. |