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Thermodynamic databases for proteins and protein–nucleic acid interactions
Author(s) -
Sarai Akinori,
Gromiha M. Michael,
An Jianghong,
Prabakaran Ponraj,
Selvaraj Samuel,
Kono Hidetoshi,
Oobatake Motohisa,
Uedaira Hatsuho
Publication year - 2001
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(2002)61:2<121::aid-bip10077>3.0.co;2-1
Subject(s) - chemistry , nucleic acid , database , chemical stability , folding (dsp implementation) , function (biology) , protein folding , biomolecule , computational biology , computer science , biochemistry , biology , organic chemistry , evolutionary biology , electrical engineering , engineering
Thermodynamicdata 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. © 2002 Wiley Periodicals, Inc. Biopoly (Nucleic Acid Sci) 61: 121–126, 2002; DOI 10.1002/bip.10077