Nucleic Acids Research, Vol 27, Issue 1 286-288, Copyright © 1999 by Oxford University Press
MM Gromiha, J An, H Kono, M Oobatake, H Uedaira and A Sarai
The first release of the Thermodynamic Database for Proteins and Mutants
(ProTherm) contains more than 3300 data of several thermodynamic parameters
for wild type and mutant proteins. Each entry includes numerical data for
unfolding Gibbs free energy change, enthalpy change, heat capacity change,
transition temperature, activity etc., which are important for
understanding the mechanism of protein stability. ProTherm also includes
structural information such as secondary structure and solvent
accessibility of wild type residues, and experimental methods and other
conditions. A WWW interface enables users to search data based on various
conditions with different sorting options for outputs. Further, ProTherm is
cross-linked with NCBI PUBMED literature database, Protein Mutant Database,
Enzyme Code and Protein Data Bank structural database. Moreover, all the
mutation sites associated with each PDB structure are automatically mapped
and can be directly viewed through 3DinSight developed in our laboratory.
The database is available at the URL,
http://www.rtc.riken.go.jp/protherm.htm l
ARTICLES
ProTherm: Thermodynamic Database for Proteins and Mutants
Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), 3-1-1 Koyadai, Tsukuba, Ibaraki 305-0074, Japan.
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