Thermodynamic databases for proteins and protein-nucleic acid interactions
| Autor: | Samuel Selvaraj, Hidetoshi Kono, Motohisa Oobatake, Akinori Sarai, Hatsuho Uedaira, Jianghong An, Ponraj Prabakaran, M. Michael Gromiha |
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| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Biophysics computer.software_genre Biochemistry Biomaterials Molecular recognition Protein stability chemistry.chemical_classification Database Chemistry Biomolecule Organic Chemistry Proteins DNA General Medicine Models Theoretical Thermodynamic database Databases as Topic Mutation Nucleic acid RNA Thermodynamics Protein folding Experimental methods computer Function (biology) Protein Binding |
| Zdroj: | Biopolymers. 61:121-126 |
| ISSN: | 1097-0282 0006-3525 |
| DOI: | 10.1002/1097-0282(2002)61:2<121::aid-bip10077>3.0.co;2-1 |
| Popis: | Thermodynamic data regarding proteins and their interactions are important for understanding the mechanisms of protein folding, protein stability, and molecular recognition. Although there are several structural databases available for proteins and their complexes with other molecules, databases for experimental thermodynamic data on protein stability and interactions are rather scarce. Thus, we have developed two electronically accessible thermodynamic databases. ProTherm, Thermodynamic Database for Proteins and Mutants, contains numerical data of several thermodynamic parameters of protein stability, experimental methods and conditions, along with structural, functional, and literature information. ProNIT, Thermodynamic Database for Protein-Nucleic Acid Interactions, contains thermodynamic data for protein-nucleic acid binding, experimental conditions, structural information of proteins, nucleic acids and the complex, and literature information. These data have been incorporated into 3DinSight, an integrated database for structure, function, and properties of biomolecules. A WWW interface allows users to search for data based on various conditions, with different display and sorting options, and to visualize molecular structures and their interactions. These thermodynamic databases, together with structural databases, help researchers gain insight into the relationship among structure, function, and thermodynamics of proteins and their interactions, and will become useful resources for studying proteins in the postgenomic era. |
| Databáze: | OpenAIRE |
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