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. 2000 Jan 1;28(1):283-5.
doi: 10.1093/nar/28.1.283.

ProTherm, version 2.0: thermodynamic database for proteins and mutants

M M Gromiha  1 , J An, H Kono, M Oobatake, H Uedaira, P Prabakaran, A Sarai
Affiliations

ProTherm, version 2.0: thermodynamic database for proteins and mutants

M M Gromiha et al. Nucleic Acids Res. .

Abstract

ProTherm 2.0 is the second release of the Thermo-dynamic Database for Proteins and Mutants that includes numerical data for several thermodynamic parameters, structural information, experimental methods and conditions, functional and literature information. The present release contains >5500 entries, an approximately 67% increase over the previous version. In addition, we have included information about reversibility of data, details about buffer and ion concentrations and the surrounding residues in space for all mutants. A WWW interface enables users to search data based on various conditions with different sorting options for outputs. Further, ProTherm has links with other structural and literature databases, and the mutation sites and surrounding residues are automatically mapped on the structures and can be directly viewed through 3DinSight developed in our laboratory. The ProTherm database is freely available through the WWW at http://www.rtc.riken.go.jp/protherm.html

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Figures

Figure 1
Figure 1
Display of protein mutants and surrounding residues by RasMol. As an example, we show the surrounding residues of Lys 91 in Ribonuclease H (2RN2). The central residue, surrounding residues within 4 Å and surrounding residues between 4 and 8 Å are shown in red, yellow and green, respectively.
See this image and copyright information in PMC

References

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Publication types