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A molecular dynamics study of acylphosphatase in aggregation‐promoting conditions: The influence of trifluoroethanol/water solvent
Author(s) -
Flöck Dagmar,
Daidone Isabella,
Di Nola Alfredo
Publication year - 2004
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20166
Subject(s) - chemistry , molecular dynamics , protein aggregation , folding (dsp implementation) , protein folding , aqueous solution , solvent , residue (chemistry) , protein structure , biophysics , computational chemistry , biochemistry , organic chemistry , electrical engineering , biology , engineering
The 98‐residue protein acylphosphatase exhibits a high propensity for aggregation under certain conditions. Aggregates formed from wild‐type acylphosphatase in the presence of 2,2,2‐trifluoroethanol and from highly destabilized mutants are essentially identical in structure. Furthermore, it has been shown by mutational studies that different regions of the protein are important for aggregation and folding. In the present molecular dynamics study, we compare the behavior of the protein in aqueous solution and in a 25 % (v/v) 2,2,2‐trifluoroethanol/water environment mimicking the experimental conditions. The 2,2,2‐trifluoroethanol surrounding affects the structure of the protein mostly in the regions important for aggregation, in good agreement with experimental data. This suggests that the early step of (partly) unfolding, which precedes the aggregation process, has been observed. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004