Thermodynamic database for proteins: features and applications
- PMID: 20221915
- DOI: 10.1007/978-1-60327-241-4_6
Thermodynamic database for proteins: features and applications
Abstract
We have developed a thermodynamic database for proteins and mutants, ProTherm, which is a collection of a large number of thermodynamic data on protein stability along with the sequence and structure information, experimental methods and conditions, and literature information. This is a valuable resource for understanding/predicting the stability of proteins, and it can be accessible at http://www.gibk26.bse.kyutech.ac.jp/jouhou/Protherm/protherm.html . ProTherm has several features including various search, display, and sorting options and visualization tools. We have analyzed the data in ProTherm to examine the relationship among thermodynamics, structure, and function of proteins. We describe the progress on the development of methods for understanding/predicting protein stability, such as (i) relationship between the stability of protein mutants and amino acid properties, (ii) average assignment method, (iii) empirical energy functions, (iv) torsion, distance, and contact potentials, and (v) machine learning techniques. The list of online resources for predicting protein stability has also been provided.
Similar articles
-
ProTherm, version 4.0: thermodynamic database for proteins and mutants.Nucleic Acids Res. 2004 Jan 1;32(Database issue):D120-1. doi: 10.1093/nar/gkh082. Nucleic Acids Res. 2004. PMID: 14681373 Free PMC article.
-
Prediction of protein stability upon point mutations.Biochem Soc Trans. 2007 Dec;35(Pt 6):1569-73. doi: 10.1042/BST0351569. Biochem Soc Trans. 2007. PMID: 18031268 Review.
-
ProTherm and ProNIT: thermodynamic databases for proteins and protein-nucleic acid interactions.Nucleic Acids Res. 2006 Jan 1;34(Database issue):D204-6. doi: 10.1093/nar/gkj103. Nucleic Acids Res. 2006. PMID: 16381846 Free PMC article.
-
Protein domain architectures.Methods Mol Biol. 2010;609:83-95. doi: 10.1007/978-1-60327-241-4_5. Methods Mol Biol. 2010. PMID: 20221914
-
Databases of protein-protein interactions and complexes.Methods Mol Biol. 2010;609:145-59. doi: 10.1007/978-1-60327-241-4_9. Methods Mol Biol. 2010. PMID: 20221918 Review.
Cited by
-
A coarse-grained elastic network atom contact model and its use in the simulation of protein dynamics and the prediction of the effect of mutations.PLoS Comput Biol. 2014 Apr 24;10(4):e1003569. doi: 10.1371/journal.pcbi.1003569. eCollection 2014 Apr. PLoS Comput Biol. 2014. PMID: 24762569 Free PMC article.
-
Utilizing natural diversity to evolve protein function: applications towards thermostability.Curr Opin Chem Biol. 2011 Jun;15(3):399-406. doi: 10.1016/j.cbpa.2011.03.005. Epub 2011 Apr 4. Curr Opin Chem Biol. 2011. PMID: 21470898 Free PMC article. Review.
-
Global computational mutagenesis provides a critical stability framework in protein structures.PLoS One. 2017 Dec 7;12(12):e0189064. doi: 10.1371/journal.pone.0189064. eCollection 2017. PLoS One. 2017. PMID: 29216252 Free PMC article.
-
Predicting folding free energy changes upon single point mutations.Bioinformatics. 2012 Mar 1;28(5):664-71. doi: 10.1093/bioinformatics/bts005. Epub 2012 Jan 11. Bioinformatics. 2012. PMID: 22238268 Free PMC article.
-
Analyses of Mutation Displacements from Homology Models.Methods Mol Biol. 2023;2627:195-210. doi: 10.1007/978-1-0716-2974-1_11. Methods Mol Biol. 2023. PMID: 36959449
MeSH terms
Substances
LinkOut - more resources
Full Text Sources