| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-57 |
Sentence |
denotes |
Development of enzymatic activity during protein folding. |
| T2 |
58-149 |
Sentence |
denotes |
Detection of a spectroscopically silent native-like intermediate of muscle acylphosphatase. |
| T3 |
150-413 |
Sentence |
denotes |
The recovery of enzymatic activity during the folding of muscle acylphosphatase and two single residue mutants (proline 54 to alanine and proline 71 to alanine) from 7 M urea has been monitored and compared with the development of intrinsic fluorescence emission. |
| T4 |
414-564 |
Sentence |
denotes |
Fluorescence measurements reveal the presence in the wild-type protein of a major rapid refolding phase followed by a second low amplitude slow phase. |
| T5 |
565-780 |
Sentence |
denotes |
The slow phase is absent in the fluorescence trace acquired with the proline 54 to alanine mutant, suggesting the involvement of this proline residue in the fluorescence-detected slow phase of the wild-type protein. |
| T6 |
781-959 |
Sentence |
denotes |
The major kinetic phase is associated with a considerable recovery of enzymatic activity, indicating that a large fraction of molecules refolds with effective two-state behavior. |
| T7 |
960-1134 |
Sentence |
denotes |
The use of time-resolved enzymatic activity as a probe to follow the folding process reveals, however, the presence of another exponential slow phase arising from proline 71. |
| T8 |
1135-1343 |
Sentence |
denotes |
This slow phase is not observable by utilizing optical probes, indicating that, unlike proline 54, the cis to trans isomerization of proline 71 can take place in an intermediate possessing a native-like fold. |
| T9 |
1344-1584 |
Sentence |
denotes |
We suggest that, although spectroscopically silent and structurally insignificant, the cis-trans interconversion of proline residues in native-like intermediates may be crucial for the generation of enzymatic activity of functional enzymes. |
