An alternative approach in the structure-based predictions of the thermodynamics of protein unfolding.
A new approach for a first-order prediction of the thermodynamic properties of small globular proteins has been developed. The method put forward here has been shown to be successful in predicting, within acceptable margins of uncertainty, the denaturational heat capacity changes of a given protein if its amino acid composition is known. If compared with other models this method has the following advantages: (1) no details about the three-dimensional structure of the protein are required; (2) comparison with the thermodynamic properties of small model compounds is not necessary; (3) the temperature dependence of the denaturational heat capacity change is taken into account. Moreover, the equations developed have allowed us to point out the errors that can be made if the temperature-dependence of the denaturational heat capacity change is not taken into account in the calculation of the unfolding thermodynamic functions.
Milardi
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Dipartimento di Scienze Chimiche, Università degli Studi di Catania, Italy.
la Rosa
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Fasone
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Grasso
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D000596:Amino Acids / Q000032:analysis / Q000737:chemistry; D003574:Cytochrome c Group / Q000737:chemistry; D008432:Mathematical Computing; D009113:Muramidase / Q000737:chemistry; D009211:Myoglobin / Q000737:chemistry; D011237:Predictive Value of Tests; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D000596:Amino Acids; D003574:Cytochrome c Group; D009211:Myoglobin; D011506:Proteins; D012259:Ribonuclease, Pancreatic; D009113:Muramidase