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Refining the treatment of membrane proteins by coarse-grained models.
- Source :
-
Proteins [Proteins] 2016 Jan; Vol. 84 (1), pp. 92-117. Date of Electronic Publication: 2015 Dec 09. - Publication Year :
- 2016
-
Abstract
- Obtaining a quantitative description of the membrane proteins stability is crucial for understanding many biological processes. However the advance in this direction has remained a major challenge for both experimental studies and molecular modeling. One of the possible directions is the use of coarse-grained models but such models must be carefully calibrated and validated. Here we use a recent progress in benchmark studies on the energetics of amino acid residue and peptide membrane insertion and membrane protein stability in refining our previously developed coarse-grained model (Vicatos et al., Proteins 2014;82:1168). Our refined model parameters were fitted and/or tested to reproduce water/membrane partitioning energetics of amino acid side chains and a couple of model peptides. This new model provides a reasonable agreement with experiment for absolute folding free energies of several β-barrel membrane proteins as well as effects of point mutations on a relative stability for one of those proteins, OmpLA. The consideration and ranking of different rotameric states for a mutated residue was found to be essential to achieve satisfactory agreement with the reference data.<br /> (© 2015 Wiley Periodicals, Inc.)
- Subjects :
- Amino Acids chemistry
Bacterial Outer Membrane Proteins chemistry
Databases, Protein
Escherichia coli chemistry
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Phospholipases A1 chemistry
Protein Folding
Protein Stability
Protein Structure, Secondary
Static Electricity
Thermodynamics
Membrane Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1097-0134
- Volume :
- 84
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Proteins
- Publication Type :
- Academic Journal
- Accession number :
- 26531155
- Full Text :
- https://doi.org/10.1002/prot.24958