Data mining the protein data bank to identify and characterise chameleon coil sequences that form symmetric homodimer [beta]-sheet interfaces

Johanna Laibe; Melanie Broutin; Aaron Caffrey; Barbara Pierscionek; Jean-Christophe Nebel

doi:10.1007/978-3-319-56154-7

Data mining the protein data bank to identify and characterise chameleon coil sequences that form symmetric homodimer [beta]-sheet interfaces

Johanna Laibe
, Melanie Broutin
, Aaron Caffrey
, Barbara Pierscionek
, Jean-Christophe Nebel

Kingston University
Université Côte d'Azur

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › peer-review

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Abstract

A protein’s environment may affect its secondary structure. In this study, the focus is on homodimers with symmetric β-sheet interfaces resulting from the conversion of coil sequences into β-strands. All homodimers in the Protein Data Bank relying on those chameleon sequences have been identified. Initial analysis based on sequential and structural features has revealed that many of those dimers display specific properties which could contribute to their detection. Such result is important since it could provide some insight on dimerisation and possibly aggregation mechanisms.

Original language	English
Title of host publication	Bioinformatics and Biomedical Engineering
Subtitle of host publication	5th International Work-Conference, IWBBIO 2017, Granada, Spain, April 26–28, 2017, Proceedings, Part II
Editors	Ignacio Rojas, Francisco Ortuno
Place of Publication	Cham
Publisher	Springer Nature
Pages	118–126
Volume	2
ISBN (Electronic)	9783319561530
DOIs	https://doi.org/10.1007/978-3-319-56154-7
Publication status	Published - 1 Apr 2017
Event	Bioinformatics and Biomedical Engineering : 5th International Work-Conference, IWBBIO 2017 - Granada, Spain Duration: 26 Apr 2017 → 28 Apr 2017

Publication series

Name	Lecture Notes in Computer Science
Volume	10209
ISSN (Print)	0302-9743
ISSN (Electronic)	1611-3349

Conference

Conference	Bioinformatics and Biomedical Engineering
Abbreviated title	IWBBIO 2017
Country/Territory	Spain
City	Granada
Period	26/04/17 → 28/04/17

Keywords

Biological sciences

Access to Document

10.1007/978-3-319-56154-7

Laibe-J-36634-AAMAccepted author manuscript, 637 KBLicence: Unspecified

Protein Bioinformatics: Structure and Function
Nebel, J.-C. (PI), Abbass, J. (CoI), Esmaielbeiki, R. (Researcher), Laibe, J. (Researcher), Dyrka, W. (Researcher), Kotulska, M. (CoI) & Konopka, B. M. (Researcher)
7/06/04 → 10/12/21
Project: Research

Cite this

Laibe, J., Broutin, M., Caffrey, A., Pierscionek, B., & Nebel, J.-C. (2017). Data mining the protein data bank to identify and characterise chameleon coil sequences that form symmetric homodimer [beta]-sheet interfaces. In I. Rojas, & F. Ortuno (Eds.), Bioinformatics and Biomedical Engineering: 5th International Work-Conference, IWBBIO 2017, Granada, Spain, April 26–28, 2017, Proceedings, Part II (Vol. 2, pp. 118–126). (Lecture Notes in Computer Science; Vol. 10209). Springer Nature. https://doi.org/10.1007/978-3-319-56154-7

Laibe, Johanna ; Broutin, Melanie ; Caffrey, Aaron et al. / Data mining the protein data bank to identify and characterise chameleon coil sequences that form symmetric homodimer [beta]-sheet interfaces. Bioinformatics and Biomedical Engineering: 5th International Work-Conference, IWBBIO 2017, Granada, Spain, April 26–28, 2017, Proceedings, Part II. editor / Ignacio Rojas ; Francisco Ortuno. Vol. 2 Cham : Springer Nature, 2017. pp. 118–126 (Lecture Notes in Computer Science).

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abstract = "A protein{\textquoteright}s environment may affect its secondary structure. In this study, the focus is on homodimers with symmetric β-sheet interfaces resulting from the conversion of coil sequences into β-strands. All homodimers in the Protein Data Bank relying on those chameleon sequences have been identified. Initial analysis based on sequential and structural features has revealed that many of those dimers display specific properties which could contribute to their detection. Such result is important since it could provide some insight on dimerisation and possibly aggregation mechanisms.",

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author = "Johanna Laibe and Melanie Broutin and Aaron Caffrey and Barbara Pierscionek and Jean-Christophe Nebel",

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Laibe, J, Broutin, M, Caffrey, A, Pierscionek, B & Nebel, J-C 2017, Data mining the protein data bank to identify and characterise chameleon coil sequences that form symmetric homodimer [beta]-sheet interfaces. in I Rojas & F Ortuno (eds), Bioinformatics and Biomedical Engineering: 5th International Work-Conference, IWBBIO 2017, Granada, Spain, April 26–28, 2017, Proceedings, Part II. vol. 2, Lecture Notes in Computer Science, vol. 10209, Springer Nature, Cham, pp. 118–126, Bioinformatics and Biomedical Engineering
, Granada, Spain, 26/04/17. https://doi.org/10.1007/978-3-319-56154-7

Data mining the protein data bank to identify and characterise chameleon coil sequences that form symmetric homodimer [beta]-sheet interfaces. / Laibe, Johanna; Broutin, Melanie; Caffrey, Aaron et al.
Bioinformatics and Biomedical Engineering: 5th International Work-Conference, IWBBIO 2017, Granada, Spain, April 26–28, 2017, Proceedings, Part II. ed. / Ignacio Rojas; Francisco Ortuno. Vol. 2 Cham: Springer Nature, 2017. p. 118–126 (Lecture Notes in Computer Science; Vol. 10209).

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution › peer-review

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AU - Pierscionek, Barbara

AU - Nebel, Jean-Christophe

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N2 - A protein’s environment may affect its secondary structure. In this study, the focus is on homodimers with symmetric β-sheet interfaces resulting from the conversion of coil sequences into β-strands. All homodimers in the Protein Data Bank relying on those chameleon sequences have been identified. Initial analysis based on sequential and structural features has revealed that many of those dimers display specific properties which could contribute to their detection. Such result is important since it could provide some insight on dimerisation and possibly aggregation mechanisms.

AB - A protein’s environment may affect its secondary structure. In this study, the focus is on homodimers with symmetric β-sheet interfaces resulting from the conversion of coil sequences into β-strands. All homodimers in the Protein Data Bank relying on those chameleon sequences have been identified. Initial analysis based on sequential and structural features has revealed that many of those dimers display specific properties which could contribute to their detection. Such result is important since it could provide some insight on dimerisation and possibly aggregation mechanisms.

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Laibe J, Broutin M, Caffrey A, Pierscionek B, Nebel JC. Data mining the protein data bank to identify and characterise chameleon coil sequences that form symmetric homodimer [beta]-sheet interfaces. In Rojas I, Ortuno F, editors, Bioinformatics and Biomedical Engineering: 5th International Work-Conference, IWBBIO 2017, Granada, Spain, April 26–28, 2017, Proceedings, Part II. Vol. 2. Cham: Springer Nature. 2017. p. 118–126. (Lecture Notes in Computer Science). doi: 10.1007/978-3-319-56154-7

Data mining the protein data bank to identify and characterise chameleon coil sequences that form symmetric homodimer [beta]-sheet interfaces

Abstract

Publication series

Conference

Keywords

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Projects

Protein Bioinformatics: Structure and Function

Cite this