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Automute protein free#
Casadio R, Compiani M, Fariselli P, Vivarelli F (1995) Predicting free energy contributions to the conformational stability of folded proteins from the residue sequence with radial basis function networks. A list of online resources for predicting has also been provided. We describe the recent progress on the development of methods for understanding/predicting protein stability, such as (1) general trends on mutational effects on stability, (2) relationship between the stability of protein mutants and amino acid properties, (3) applications of protein three-dimensional structures for predicting their stability upon point mutations, (4) prediction of protein stability upon single mutations from amino acid sequence, and (5) prediction methods for addressing double mutants. ProTherm has been effectively used to examine the relationship among thermodynamics, structure, and function of proteins. ProTherm is a valuable resource for understanding/predicting the stability of proteins and it can be accessed at. Different features such as search, display, and sorting options and visualization tools have been incorporated in the database. It also contains sequence and structure information of a protein, experimental methods and conditions, and literature information. These experimental data have been accumulated in the form of a database, ProTherm, thermodynamic database for proteins and mutants. Experimentally, protein stability is measured with circular dichroism, differential scanning calorimetry, and fluorescence spectroscopy using thermal and denaturant denaturation methods. Protein stability is the free energy difference between unfolded and folded states of a protein, which lies in the range of 5–25 kcal/mol.
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