| Abstract
| - Prediction of protein folding rates from amino acid sequences is one of the most important challenges inmolecular biology. In this work, I have related the protein folding rates with physical-chemical, energeticand conformational properties of amino acid residues. I found that the classification of proteins into differentstructural classes shows an excellent correlation between amino acid properties and folding rates of two-and three-state proteins, indicating the importance of native state topology in determining the protein foldingrates. I have formulated a simple linear regression model for predicting the protein folding rates from aminoacid sequences along with structural class information and obtained an excellent agreement between predictedand experimentally observed folding rates of proteins; the correlation coefficients are 0.99, 0.96 and 0.95,respectively, for all-α, all-β and mixed class proteins. This is the first available method, which is capableof predicting the protein folding rates just from the amino acid sequence with the aid of generic amino acidproperties and structural class information.
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