Dataset Information

GRAFENE: Graphlet-based alignment-free network approach integrates 3D structural and sequence (residue order) data to improve protein structural comparison.

ABSTRACT: Initial protein structural comparisons were sequence-based. Since amino acids that are distant in the sequence can be close in the 3-dimensional (3D) structure, 3D contact approaches can complement sequence approaches. Traditional 3D contact approaches study 3D structures directly and are alignment-based. Instead, 3D structures can be modeled as protein structure networks (PSNs). Then, network approaches can compare proteins by comparing their PSNs. These can be alignment-based or alignment-free. We focus on the latter. Existing network alignment-free approaches have drawbacks: 1) They rely on naive measures of network topology. 2) They are not robust to PSN size. They cannot integrate 3) multiple PSN measures or 4) PSN data with sequence data, although this could improve comparison because the different data types capture complementary aspects of the protein structure. We address this by: 1) exploiting well-established graphlet measures via a new network alignment-free approach, 2) introducing normalized graphlet measures to remove the bias of PSN size, 3) allowing for integrating multiple PSN measures, and 4) using ordered graphlets to combine the complementary PSN data and sequence (specifically, residue order) data. We compare synthetic networks and real-world PSNs more accurately and faster than existing network (alignment-free and alignment-based), 3D contact, or sequence approaches.

SUBMITTER: Faisal FE

PROVIDER: S-EPMC5668259 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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Publications

GRAFENE: Graphlet-based alignment-free network approach integrates 3D structural and sequence (residue order) data to improve protein structural comparison.

Faisal Fazle E FE Newaz Khalique K Chaney Julie L JL Li Jun J Emrich Scott J SJ Clark Patricia L PL Milenković Tijana T

Scientific reports 20171102 1

Initial protein structural comparisons were sequence-based. Since amino acids that are distant in the sequence can be close in the 3-dimensional (3D) structure, 3D contact approaches can complement sequence approaches. Traditional 3D contact approaches study 3D structures directly and are alignment-based. Instead, 3D structures can be modeled as protein structure networks (PSNs). Then, network approaches can compare proteins by comparing their PSNs. These can be alignment-based or alignment-free ...[more]

PMID: 29097661

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Project description:Alignment of large and diverse sequence sets is a common task in biological investigations, yet there remains considerable room for improvement in alignment quality. Multiple sequence alignment programs tend to reach maximal accuracy when aligning only a few sequences, and then diminish steadily as more sequences are added. This drop in accuracy can be partly attributed to a build-up of error and ambiguity as more sequences are aligned. Most high-throughput sequence alignment algorithms do not use contextual information under the assumption that sites are independent. This study examines the extent to which local sequence context can be exploited to improve the quality of large multiple sequence alignments.Two predictors based on local sequence context were assessed: (i) single sequence secondary structure predictions, and (ii) modulation of gap costs according to the surrounding residues. The results indicate that context-based predictors have appreciable information content that can be utilized to create more accurate alignments. Furthermore, local context becomes more informative as the number of sequences increases, enabling more accurate protein alignments of large empirical benchmarks. These discoveries became the basis for DECIPHER, a new context-aware program for sequence alignment, which outperformed other programs on large sequence sets.Predicting secondary structure based on local sequence context is an efficient means of breaking the independence assumption in alignment. Since secondary structure is more conserved than primary sequence, it can be leveraged to improve the alignment of distantly related proteins. Moreover, secondary structure predictions increase in accuracy as more sequences are used in the prediction. This enables the scalable generation of large sequence alignments that maintain high accuracy even on diverse sequence sets. The DECIPHER R package and source code are freely available for download at DECIPHER.cee.wisc.edu and from the Bioconductor repository.

Dataset Information

GRAFENE: Graphlet-based alignment-free network approach integrates 3D structural and sequence (residue order) data to improve protein structural comparison.

Publications

GRAFENE: Graphlet-based alignment-free network approach integrates 3D structural and sequence (residue order) data to improve protein structural comparison.

Similar Datasets

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