Insights on protein thermal stability: a graph representation of molecular interactions.


Journal

Bioinformatics (Oxford, England)
ISSN: 1367-4811
Titre abrégé: Bioinformatics
Pays: England
ID NLM: 9808944

Informations de publication

Date de publication:
01 08 2019
Historique:
received: 01 08 2018
revised: 29 10 2018
accepted: 07 12 2018
pubmed: 12 12 2018
medline: 17 6 2020
entrez: 12 12 2018
Statut: ppublish

Résumé

Understanding the molecular mechanisms of thermal stability is a challenge in protein biology. Indeed, knowing the temperature at which proteins are stable has important theoretical implications, which are intimately linked with properties of the native fold, and a wide range of potential applications from drug design to the optimization of enzyme activity. Here, we present a novel graph-theoretical framework to assess thermal stability based on the structure without any a priori information. In this approach we describe proteins as energy-weighted graphs and compare them using ensembles of interaction networks. Investigating the position of specific interactions within the 3D native structure, we developed a parameter-free network descriptor that permits to distinguish thermostable and mesostable proteins with an accuracy of 76% and area under the receiver operating characteristic curve of 78%. Code is available upon request to edoardo.milanetti@uniroma1.it. Supplementary data are available at Bioinformatics online.

Identifiants

pubmed: 30535291
pii: 5237552
doi: 10.1093/bioinformatics/bty1011
pmc: PMC6662296
doi:

Substances chimiques

Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2569-2577

Informations de copyright

© The Author(s) 2018. Published by Oxford University Press.

Références

Protein Eng. 2000 Mar;13(3):179-91
pubmed: 10775659
Nature. 2001 Feb 1;409(6820):641-5
pubmed: 11214326
Nature. 2001 Feb 22;409(6823):1092-101
pubmed: 11234023
Protein Eng. 2003 Apr;16(4):279-86
pubmed: 12736371
Biophys J. 2003 Oct;85(4):2641-9
pubmed: 14507727
Prog Nucleic Acid Res Mol Biol. 2003;74:37-81
pubmed: 14510073
Biophys J. 2004 Jan;86(1 Pt 1):85-91
pubmed: 14695252
Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3325-6
pubmed: 14993602
Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3747-52
pubmed: 15007165
Structure. 2005 Jun;13(6):857-60
pubmed: 15939017
Biophys J. 2005 Dec;89(6):4159-70
pubmed: 16150969
J Comput Chem. 2005 Dec;26(16):1781-802
pubmed: 16222654
Biophys Chem. 2006 Feb 1;119(3):256-70
pubmed: 16253416
Nucleic Acids Res. 2006 Jan 1;34(Database issue):D204-6
pubmed: 16381846
Ann N Y Acad Sci. 2005 Dec;1066:12-33
pubmed: 16533916
Protein Sci. 2006 Jul;15(7):1569-78
pubmed: 16815912
J Am Chem Soc. 2007 May 2;129(17):5374-5
pubmed: 17411056
Science. 1985 Oct 11;230(4722):132-8
pubmed: 17842674
J Chem Inf Model. 2008 Jan;48(1):119-27
pubmed: 18161956
BMC Struct Biol. 2008 Feb 29;8:14
pubmed: 18312638
Comput Biol Chem. 2009 Dec;33(6):445-50
pubmed: 19896904
Biophys J. 2010 Feb 17;98(4):667-77
pubmed: 20159163
Biophys J. 2010 Apr 7;98(7):1109-18
pubmed: 20371310
Proteins. 2010 Sep;78(12):2699-706
pubmed: 20589630
J Am Chem Soc. 2010 Nov 17;132(45):16240-6
pubmed: 20979399
Biophys J. 2010 Dec 1;99(11):3704-15
pubmed: 21112295
J Biosci. 2011 Jun;36(2):253-63
pubmed: 21654080
J Chem Inf Model. 2011 Jul 25;51(7):1623-33
pubmed: 21662246
Crit Rev Biochem Mol Biol. 1990;25(4):281-305
pubmed: 2225910
J Biomol Struct Dyn. 2012;29(5):961-71
pubmed: 22292954
J Mol Biol. 2012 Apr 13;417(5):413-24
pubmed: 22342930
J Chem Inf Model. 2012 Dec 21;52(12):3144-54
pubmed: 23146088
J Chem Inf Model. 2013 Sep 23;53(9):2448-61
pubmed: 23962324
PLoS One. 2014 Mar 19;9(3):e91659
pubmed: 24646884
Biochim Biophys Acta. 2014 Dec;1844(12):2174-81
pubmed: 25172393
Nucleic Acids Res. 2015 Jan;43(Database issue):D376-81
pubmed: 25348408
PLoS One. 2014 Nov 13;9(11):e112751
pubmed: 25393107
Chemphyschem. 2015 Dec 1;16(17):3599-602
pubmed: 26426928
Sci Rep. 2016 Mar 18;6:23257
pubmed: 26988870
Nucleic Acids Res. 2016 Jul 8;44(W1):W375-82
pubmed: 27151201
Nature. 2016 Sep 14;537(7620):320-7
pubmed: 27629638
Philos Trans A Math Phys Eng Sci. 2016 Nov 13;374(2080):
pubmed: 27698032
Curr Opin Struct Biol. 2017 Feb;42:117-128
pubmed: 28040640
Sci Rep. 2017 Apr 24;7:46568
pubmed: 28436442
Nat Commun. 2017 May 18;8:15428
pubmed: 28516908
J Biomol Struct Dyn. 2018 Sep;36(12):3265-3273
pubmed: 28952426
Bioinformatics. 2017 Nov 1;33(21):3415-3422
pubmed: 29036273
Biochemistry. 1979 Dec 11;18(25):5698-703
pubmed: 518863
Biopolymers. 1983 Dec;22(12):2577-637
pubmed: 6667333
Eur J Biochem. 1994 Mar 15;220(3):981-5
pubmed: 8143751
Proteins. 1996 Jan;24(1):81-91
pubmed: 8628735
J Mol Biol. 1997 Jun 20;269(4):631-43
pubmed: 9217266
Fold Des. 1997;2(4):S40-6
pubmed: 9269567

Auteurs

Mattia Miotto (M)

Department of Physics, Sapienza University, Piazzale Aldo Moro 5, Rome, Italy.
Center for Life Nano Science@Sapienza, Instituto Italiano di Tecnologia, Viale Regina Elena, 291 Roma (RM), Italy.
Soft and Living Matter Laboratory, Institute of Nanotechnology, Consiglio Nazionale delle Ricerche, Rome, Italy.

Pier Paolo Olimpieri (PP)

Department of Physics, Sapienza University, Piazzale Aldo Moro 5, Rome, Italy.

Lorenzo Di Rienzo (L)

Department of Physics, Sapienza University, Piazzale Aldo Moro 5, Rome, Italy.

Francesco Ambrosetti (F)

Department of Physics, Sapienza University, Piazzale Aldo Moro 5, Rome, Italy.
Bijvoet Center for Biomolecular Research, Faculty of Science - Chemistry, Utrecht University, Padualaan 8, Utrecht, the Netherlands.

Pietro Corsi (P)

Department of Science, Università degli Studi "Roma Tre", via della Vasca Navale 84, Rome, Italy.

Rosalba Lepore (R)

Biozentrum, University of Basel, Klingelbergstrasse 50-70, CH-4056 Basel, Switzerland.
SIB Swiss Institute of Bioinformatics, Biozentrum, University of Basel, Klingelbergstrasse 50-70, CH-4056 Basel, Switzerland.

Gian Gaetano Tartaglia (GG)

Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, Dr. Aiguader St. 88, Barcelona, Spain.
Institucio' Catalana de Recerca i Estudis Avancats (ICREA), 23 Passeig Lluìs Companys, Barcelona, Spain.
Department of Biology and Biotechnology, Sapienza University of Rome, Piazzale Aldo Moro 5, Rome, Italy.

Edoardo Milanetti (E)

Department of Physics, Sapienza University, Piazzale Aldo Moro 5, Rome, Italy.
Center for Life Nano Science@Sapienza, Instituto Italiano di Tecnologia, Viale Regina Elena, 291 Roma (RM), Italy.

Articles similaires

Selecting optimal software code descriptors-The case of Java.

Yegor Bugayenko, Zamira Kholmatova, Artem Kruglov et al.
1.00
Software Algorithms Programming Languages
Databases, Protein Protein Domains Protein Folding Proteins Deep Learning
1.00
Humans Magnetic Resonance Imaging Brain Infant, Newborn Infant, Premature
Humans Colorectal Neoplasms Biomarkers, Tumor Prognosis Gene Expression Regulation, Neoplastic

Classifications MeSH