Abstract
Comparing two or more protein structures with respect to their degree of folding is common practice in structural biology despite the fact that there is no scale for a folding degree. Here we introduce a formal definition of a folding degree, capable of quantitative characterization. This enables ordering among protein chains based on their degree of folding. The folding degree of a data set of 152 representative nonhomologous proteins is then studied. We demonstrate that the variation in the folding degree seen for this data set is not due to crystallization artifacts or experimental conditions, such as resolution, refinement protocol, pH, or temperature. A good linear relationship is observed between the folding degree and the percentages of secondary structures in the protein. The folding degree is able to account for the small changes produced in the structure due to crystal packing and temperature. Automating the classification of proteins into their respective structural domain classes, namely mainly-alpha, mainly-beta, and alpha-beta, is also possible.
Published Version
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