Dataset Information

Predicting Designability of Small Proteins from Graph Features of Contact Maps.

ABSTRACT: Highly designable structures can be distinguished based on certain geometric graphical features of the interactions, confirming the fact that the topology of a protein structure and its residue-residue interaction network are important determinants of its designability. The most designable structures and least designable structures obtained for sets of proteins having the same number of residues are compared. It is shown that the most designable structures predicted by the graph features of the contact diagrams are more densely packed, whereas the poorly designable structures are more open structures or structures that are loosely packed. Interestingly enough, it can also be seen that the highly designable identified are also common structural motifs found in nature.

SUBMITTER: Leelananda SP

PROVIDER: S-EPMC4876523 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature

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Predicting Designability of Small Proteins from Graph Features of Contact Maps.

Leelananda Sumudu P SP Jernigan Robert L RL Kloczkowski Andrzej A

Journal of computational biology : a journal of computational molecular cell biology 20160501 5

Highly designable structures can be distinguished based on certain geometric graphical features of the interactions, confirming the fact that the topology of a protein structure and its residue-residue interaction network are important determinants of its designability. The most designable structures and least designable structures obtained for sets of proteins having the same number of residues are compared. It is shown that the most designable structures predicted by the graph features of the ...[more]

PMID: 27159634

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Project description:BACKGROUND:The residue-wise contact order (RWCO) describes the sequence separations between the residues of interest and its contacting residues in a protein sequence. It is a new kind of one-dimensional protein structure that represents the extent of long-range contacts and is considered as a generalization of contact order. Together with secondary structure, accessible surface area, the B factor, and contact number, RWCO provides comprehensive and indispensable important information to reconstructing the protein three-dimensional structure from a set of one-dimensional structural properties. Accurately predicting RWCO values could have many important applications in protein three-dimensional structure prediction and protein folding rate prediction, and give deep insights into protein sequence-structure relationships. RESULTS:We developed a novel approach to predict residue-wise contact order values in proteins based on support vector regression (SVR), starting from primary amino acid sequences. We explored seven different sequence encoding schemes to examine their effects on the prediction performance, including local sequence in the form of PSI-BLAST profiles, local sequence plus amino acid composition, local sequence plus molecular weight, local sequence plus secondary structure predicted by PSIPRED, local sequence plus molecular weight and amino acid composition, local sequence plus molecular weight and predicted secondary structure, and local sequence plus molecular weight, amino acid composition and predicted secondary structure. When using local sequences with multiple sequence alignments in the form of PSI-BLAST profiles, we could predict the RWCO distribution with a Pearson correlation coefficient (CC) between the predicted and observed RWCO values of 0.55, and root mean square error (RMSE) of 0.82, based on a well-defined dataset with 680 protein sequences. Moreover, by incorporating global features such as molecular weight and amino acid composition we could further improve the prediction performance with the CC to 0.57 and an RMSE of 0.79. In addition, combining the predicted secondary structure by PSIPRED was found to significantly improve the prediction performance and could yield the best prediction accuracy with a CC of 0.60 and RMSE of 0.78, which provided at least comparable performance compared with the other existing methods. CONCLUSION:The SVR method shows a prediction performance competitive with or at least comparable to the previously developed linear regression-based methods for predicting RWCO values. In contrast to support vector classification (SVC), SVR is very good at estimating the raw value profiles of the samples. The successful application of the SVR approach in this study reinforces the fact that support vector regression is a powerful tool in extracting the protein sequence-structure relationship and in estimating the protein structural profiles from amino acid sequences.

Dataset Information

Predicting Designability of Small Proteins from Graph Features of Contact Maps.

Publications

Predicting Designability of Small Proteins from Graph Features of Contact Maps.

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