Thermodynamic database for proteins: features and applications.
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.
Gromiha
M Michael
MM
Computational Biology Research Center, National Institute of Advanced Industrial Science and Technology, Tokyo, Japan.
Sarai
Akinori
A
D000595:Amino Acid Sequence; D000818:Animals; D001185:Artificial Intelligence; D003196:Computer Graphics; D057225:Data Mining; D030562:Databases, Protein; D006801:Humans; D020407:Internet; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D012984:Software; D013329:Structure-Activity Relationship; D049490:Systems Biology; D018511:Systems Integration; D009626:Terminology as Topic; D013816:Thermodynamics; D014584:User-Computer Interface
D011506:Proteins