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Bi-factor analysis based on noise-reduction (BIFANR): a new algorithm for detecting coevolving amino acid sites in proteins.

ABSTRACT: Previous statistical analyses have shown that amino acid sites in a protein evolve in a correlated way instead of independently. Even though located distantly in the linear sequence, the coevolved amino acids could be spatially adjacent in the tertiary structure, and constitute specific protein sectors. Moreover, these protein sectors are independent of one another in structure, function, and even evolution. Thus, systematic studies on protein sectors inside a protein will contribute to the clarification of protein function. In this paper, we propose a new algorithm BIFANR (Bi-factor Analysis Based on Noise-reduction) for detecting protein sectors in amino acid sequences. After applying BIFANR on S1A family and PDZ family, we carried out internal correlation test, statistical independence test, evolutionary rate analysis, evolutionary independence analysis, and function analysis to assess the prediction. The results showed that the amino acids in certain predicted protein sector are closely correlated in structure, function, and evolution, while protein sectors are nearly statistically independent. The results also indicated that the protein sectors have distinct evolutionary directions. In addition, compared with other algorithms, BIFANR has higher accuracy and robustness under the influence of noise sites.

SUBMITTER: Liu J

PROVIDER: S-EPMC3835919 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Bi-factor analysis based on noise-reduction (BIFANR): a new algorithm for detecting coevolving amino acid sites in proteins.

Liu Juntao J Duan Xiaoyun X Sun Jianyang J Yin Yanbin Y Li Guojun G Wang Lushan L Liu Bingqiang B

PloS one 20131120 11

Previous statistical analyses have shown that amino acid sites in a protein evolve in a correlated way instead of independently. Even though located distantly in the linear sequence, the coevolved amino acids could be spatially adjacent in the tertiary structure, and constitute specific protein sectors. Moreover, these protein sectors are independent of one another in structure, function, and even evolution. Thus, systematic studies on protein sectors inside a protein will contribute to the clar ...[more]

PMID: 24278175

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Project description:Understanding the molecular details of protein-DNA interactions is critical for deciphering the mechanisms of gene regulation. We present a machine learning approach for the identification of amino acid residues involved in protein-DNA interactions.We start with a Naïve Bayes classifier trained to predict whether a given amino acid residue is a DNA-binding residue based on its identity and the identities of its sequence neighbors. The input to the classifier consists of the identities of the target residue and 4 sequence neighbors on each side of the target residue. The classifier is trained and evaluated (using leave-one-out cross-validation) on a non-redundant set of 171 proteins. Our results indicate the feasibility of identifying interface residues based on local sequence information. The classifier achieves 71% overall accuracy with a correlation coefficient of 0.24, 35% specificity and 53% sensitivity in identifying interface residues as evaluated by leave-one-out cross-validation. We show that the performance of the classifier is improved by using sequence entropy of the target residue (the entropy of the corresponding column in multiple alignment obtained by aligning the target sequence with its sequence homologs) as additional input. The classifier achieves 78% overall accuracy with a correlation coefficient of 0.28, 44% specificity and 41% sensitivity in identifying interface residues. Examination of the predictions in the context of 3-dimensional structures of proteins demonstrates the effectiveness of this method in identifying DNA-binding sites from sequence information. In 33% (56 out of 171) of the proteins, the classifier identifies the interaction sites by correctly recognizing at least half of the interface residues. In 87% (149 out of 171) of the proteins, the classifier correctly identifies at least 20% of the interface residues. This suggests the possibility of using such classifiers to identify potential DNA-binding motifs and to gain potentially useful insights into sequence correlates of protein-DNA interactions.Naïve Bayes classifiers trained to identify DNA-binding residues using sequence information offer a computationally efficient approach to identifying putative DNA-binding sites in DNA-binding proteins and recognizing potential DNA-binding motifs.

Project description:BackgroundQuantum noise intrinsically limits the quality of fluoroscopic images. The lower is the X-ray dose the higher is the noise. Fluoroscopy video processing can enhance image quality and allows further patient's dose lowering. This study aims to assess the performances achieved by a Noise Variance Conditioned Average (NVCA) spatio-temporal filter for real-time denoising of fluoroscopic sequences. The filter is specifically designed for quantum noise suppression and edge preservation. It is an average filter that excludes neighborhood pixel values exceeding noise statistic limits, by means of a threshold which depends on the local noise standard deviation, to preserve the image spatial resolution. The performances were evaluated in terms of contrast-to-noise-ratio (CNR) increment, image blurring (full width of the half maximum of the line spread function) and computational time. The NVCA filter performances were compared to those achieved by simple moving average filters and the state-of-the-art video denoising block matching-4D (VBM4D) algorithm. The influence of the NVCA filter size and threshold on the final image quality was evaluated too.ResultsFor NVCA filter mask size of 5 × 5 × 5 pixels (the third dimension represents the temporal extent of the filter) and a threshold level equal to 2 times the local noise standard deviation, the NVCA filter achieved a 10% increase of the CNR with respect to the unfiltered sequence, while the VBM4D achieved a 14% increase. In the case of NVCA, the edge blurring did not depend on the speed of the moving objects; on the other hand, the spatial resolution worsened of about 2.2 times by doubling the objects speed with VBM4D. The NVCA mask size and the local noise-threshold level are critical for final image quality. The computational time of the NVCA filter was found to be just few percentages of that required for the VBM4D filter.ConclusionsThe NVCA filter obtained a better image quality compared to simple moving average filters, and a lower but comparable quality when compared with the VBM4D filter. The NVCA filter showed to preserve edge sharpness, in particular in the case of moving objects (performing even better than VBM4D). The simplicity of the NVCA filter and its low computational burden make this filter suitable for real-time video processing and its hardware implementation is ready to be included in future fluoroscopy devices, offering further lowering of patient's X-ray dose.

Dataset Information

Bi-factor analysis based on noise-reduction (BIFANR): a new algorithm for detecting coevolving amino acid sites in proteins.

Publications

Bi-factor analysis based on noise-reduction (BIFANR): a new algorithm for detecting coevolving amino acid sites in proteins.

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