Proteins folding patterns

The secondary and tertiary protein folding patterns. This could, for example control the conformational flexibility and the resistance of proteins to unfolding. Conformationally soft proteins would, for example, be expected to generally exhibit stronger surface affinity than rigid proteins. 

One approach to the protein structure prediction is to classify the folding patterns of globular proteins. This is based on the observation from examining known tertiary structures that the variety of protein folding patterns is significantly restricted. Therefore, it is likely that a protein may belong to one of the previously identified folding patterns. 

Dubchak, I., Holbrook, S. R. Kim, S.-H. (1993b). Comparison of two variations of neural network approach to the prediction of protein folding pattern. Ismb 1,118-26. 

After fructose-1,6-bisphosphate is cleaved by aldolase to afford dihydroxyacetone phosphate (122) and glyceraldehyde-3-phosphate (124), the former is further converted to the latter by trlosephosphate isomerase (TIM). The structure of this enzyme has the prototypical TIM fold as an (a/ )s barrel (Figure 12), with the active site in one side of the barrel. This protein folding pattern is also found in the structures of hexose isomerases. 

C. Chothia and A.V. Finkelstein. 1990. The classification and origin of protein folding patterns Rev. Biochem. 59 1007-1039. (PubMed)... 

C. Chothia and A. V. Finkelstein. The classifications and origins of protein folding patterns. Annual Review of Biochemistry, 59 (1990), 1007. 

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