The hsp70 family of major stress proteins is composed of several different members exhibiting similar structural and functional properties. In order to obtain an antiserum with wide epitope reactivity, rabbits were immunized with a mixture of native and denatured hsp70 purified from bovine muscle by
A predicted consensus structure for the N-Terminal fragment of the heat shock protein HSP90 family
✍ Scribed by Dietlind L. Gerloff; Fred E. Cohen; Chantal Korostensky; Marcel Turcotte; Gaston H. Gonnet; Steven A. Benner
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 48 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0887-3585
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✦ Synopsis
A secondary structure has been predicted for the heat shock protein HSP90 family from an aligned set of homologous protein sequences by using a transparent method in both manual and automated implementation that extracts conformational information from patterns of variation and conservation within the family. No statistically significant sequence similarity relates this family to any protein with known crystal structure. However, the secondary structure prediction, together with the assignment of active site positions and possible biochemical properties, suggest that the fold is similar to that seen in N-terminal domain of DNA gyrase B (the ATPase fragment). Proteins 27:450-458, 1997.
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