Evidence map›Paper›PMID 35744836›Full record

ArticleMolecules (Basel, Switzerland)2022

CRFalign: A Sequence-Structure Alignment of Proteins Based on a Combination of HMM-HMM Comparison and Conditional Random Fields.

Sung Jong Lee, Keehyoung Joo, Sangjin Sim, Juyong Lee, In-Ho Lee, Jooyoung Lee

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Sung Jong LeeBasic Science Institute, Changwon National University, Changwon 51140, Korea.
Keehyoung JooCenter for Advanced Computation, Korea Institute for Advanced Study, Seoul 02455, Korea.
Sangjin SimNAVER CLOVA, Seongnam 13561, Korea.
Juyong LeeDepartment of Chemistry, Kangwon National University, Chuncheon 24341, Korea.ORCID 0000-0003-1174-4358
In-Ho LeeKorea Research Institute of Standards and Science (KRISS), Daejeon 34113, Korea.
Jooyoung LeeSchool of Computational Sciences, Korea Institute for Advanced Study, Seoul 02455, Korea.

Funding

Ministry of Science and ICT, KOREA NRF-2017R1E1A1A01077717, NRF-2018R1D1A1B07049312
6 · The paper itself

Abstract

Sequence-structure alignment for protein sequences is an important task for the template-based modeling of 3D structures of proteins. Building a reliable sequence-structure alignment is a challenging problem, especially for remote homologue target proteins. We built a method of sequence-structure alignment called CRFalign, which improves upon a base alignment model based on HMM-HMM comparison by employing pairwise conditional random fields in combination with nonlinear scoring functions of structural and sequence features. Nonlinear scoring part is implemented by a set of gradient boosted regression trees. In addition to sequence profile features, various position-dependent structural features are employed including secondary structures and solvent accessibilities. Training is performed on reference alignments at superfamily levels or twilight zone chosen from the SABmark benchmark set. We found that CRFalign method produces relative improvement in terms of average alignment accuracies for validation sets of SABmark benchmark. We also tested CRFalign on 51 sequence-structure pairs involving 15 FM target domains of CASP14, where we could see that CRFalign leads to an improvement in average modeling accuracies in these hard targets (TM-CRFalign ≃42.94%) compared with that of HHalign (TM-HHalign ≃39.05%) and also that of MRFalign (TM-MRFalign ≃36.93%). CRFalign was incorporated to our template search framework called CRFpred and was tested for a random target set of 300 target proteins consisting of Easy, Medium and Hard sets which showed a reasonable template search performance.

Indexed as

AlgorithmsProteinsAmino Acid SequenceProtein Structure, SecondarySequence AlignmentSolventsProteinsSolventsboosted regression treesCASPconditional random fieldsprotein structure predictionsequence-structure alignmenttemplate-based modeling

Identifiers

PMID35744836
PMCPMC9231382

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.