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Relevant bibliographies by topics / Protein sequence alignment

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Journal articles

Academic literature on the topic 'Protein sequence alignment'

Author: Grafiati

Published: 14 March 2023

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Journal articles on the topic "Protein sequence alignment"

1

Staritzbichler, René, Edoardo Sarti, Emily Yaklich, et al. "Refining pairwise sequence alignments of membrane proteins by the incorporation of anchors." PLOS ONE 16, no. 4 (2021): e0239881. http://dx.doi.org/10.1371/journal.pone.0239881.

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The alignment of primary sequences is a fundamental step in the analysis of protein structure, function, and evolution, and in the generation of homology-based models. Integral membrane proteins pose a significant challenge for such sequence alignment approaches, because their evolutionary relationships can be very remote, and because a high content of hydrophobic amino acids reduces their complexity. Frequently, biochemical or biophysical data is available that informs the optimum alignment, for example, indicating specific positions that share common functional or structural roles. Currently

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2

Pervez, Muhammad Tariq, Hayat Ali Shah, Masroor Ellahi Babar, Nasir Naveed, and Muhammad Shoaib. "SAliBASE: A Database of Simulated Protein Alignments." Evolutionary Bioinformatics 15 (January 2019): 117693431882108. http://dx.doi.org/10.1177/1176934318821080.

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Simulated alignments are alternatives to manually constructed multiple sequence alignments for evaluating performance of multiple sequence alignment tools. The importance of simulated sequences is recognized because their true evolutionary history is known, which is very helpful for reconstructing accurate phylogenetic trees and alignments. However, generating simulated alignments require expertise to use bioinformatics tools and consume several hours for reconstructing even a few hundreds of simulated sequences. It becomes a tedious job for an end user who needs a few datasets of variety of s

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3

Cavanaugh, David, and Krishnan Chittur. "A hydrophobic proclivity index for protein alignments." F1000Research 4 (October 21, 2015): 1097. http://dx.doi.org/10.12688/f1000research.6348.1.

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Sequence alignment algorithms are fundamental to modern bioinformatics. Sequence alignments are widely used in diverse applications such as phylogenetic analysis, database searches for related sequences to aid identification of unknown protein domain structures and classification of proteins and protein domains. Additionally, alignment algorithms are integral to the location of related proteins to secure understanding of unknown protein functions, to suggest the folded structure of proteins of unknown structure from location of homologous proteins and/or by locating homologous domains of known

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4

Cavanaugh, David, and Krishnan Chittur. "A hydrophobic proclivity index for protein alignments." F1000Research 4 (October 15, 2020): 1097. http://dx.doi.org/10.12688/f1000research.6348.2.

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Sequence alignment algorithms are fundamental to modern bioinformatics. Sequence alignments are widely used in diverse applications such as phylogenetic analysis, database searches for related sequences to aid identification of unknown protein domain structures and classification of proteins and protein domains. Additionally, alignment algorithms are integral to the location of related proteins to secure understanding of unknown protein functions, to suggest the folded structure of proteins of unknown structure from location of homologous proteins and/or by locating homologous domains of known

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5

Aadland, Kelsey, and Bryan Kolaczkowski. "Alignment-Integrated Reconstruction of Ancestral Sequences Improves Accuracy." Genome Biology and Evolution 12, no. 9 (2020): 1549–65. http://dx.doi.org/10.1093/gbe/evaa164.

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Abstract Ancestral sequence reconstruction (ASR) uses an alignment of extant protein sequences, a phylogeny describing the history of the protein family and a model of the molecular-evolutionary process to infer the sequences of ancient proteins, allowing researchers to directly investigate the impact of sequence evolution on protein structure and function. Like all statistical inferences, ASR can be sensitive to violations of its underlying assumptions. Previous studies have shown that, whereas phylogenetic uncertainty has only a very weak impact on ASR accuracy, uncertainty in the protein se

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6

Barton, Geoffrey J. "Protein Sequence Alignment Techniques." Acta Crystallographica Section D Biological Crystallography 54, no. 6 (1998): 1139–46. http://dx.doi.org/10.1107/s0907444998008324.

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The basic algorithms for alignment of two or more protein sequences are explained. Alternative methods for scoring substitutions and gaps (insertions and deletions) are described, as are global and local alignment methods. Multiple alignment techniques are explained, including methods for profile comparison. A summary is given of programs for the alignment and analysis of protein sequences, either from sequence alone, or from three-dimensional structure.

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7

Kanagarajadurai, Karuppiah, Singaravelu Kalaimathy, Paramasivam Nagarajan, and Ramanathan Sowdhamini. "PASS2." International Journal of Knowledge Discovery in Bioinformatics 2, no. 4 (2011): 53–66. http://dx.doi.org/10.4018/jkdb.2011100104.

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A detailed comparison of protein domains that belong to families and superfamilies shows that structure is better conserved than sequence during evolutionary divergence. Sequence alignments, guided by structural features, permit a better sampling of the protein sequence space and effective construction of libraries for fold recognition. Sequence alignments are useful evolutionary models in defining structure-function relationships for protein superfamilies. The PASS2 database, maintained by the authors, presents alignments of proteins related at the superfamily level and characterised by low s

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8

Pei, Jimin. "Multiple protein sequence alignment." Current Opinion in Structural Biology 18, no. 3 (2008): 382–86. http://dx.doi.org/10.1016/j.sbi.2008.03.007.

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9

PAI, TUN-WEN, RUEI-HSIANG CHANG, CHIEN-MING CHEN, et al. "MULTIPLE STRUCTURE ALIGNMENT BASED ON GEOMETRICAL CORRELATION OF SECONDARY STRUCTURE ELEMENTS." New Mathematics and Natural Computation 06, no. 01 (2010): 77–95. http://dx.doi.org/10.1142/s1793005710001621.

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Protein structure alignment facilitates the analysis of protein functionality. Through superimposed structures and the comparison of variant components, common or specific features of proteins can be identified. Several known protein families exhibit analogous tertiary structures but divergent primary sequences. These proteins in the same structural class are unable to be aligned by sequence-based methods. The main objective of the present study was to develop an efficient and effective algorithm for multiple structure alignment based on geometrical correlation of secondary structures, which a

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10

Henneke, Christina M., Michael J. Danson, David W. Hough, and David J. Osguthorpe. "Sequence alignment of citrate synthase proteins using a multiple sequence alignment algorithm and multiple scoring matrices." "Protein Engineering, Design and Selection" 2, no. 8 (1989): 597–604. http://dx.doi.org/10.1093/protein/2.8.597.

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