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 t
A predicted consensus structure for the C terminus of the beta and gamma chains of fibrinogen
β Scribed by Dietlind L. Gerloff; Fred E. Cohen; Steven A. Benner
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 432 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
β¦ Synopsis
A secondary structure has been predicted for the C termini of the fibrinogen b and g chains from an aligned set of homologous protein sequences using a transparent method that extracts conformational information from patters of variation and conservation, parsing strings, and patterns of amphiphilicity. The structure is modeled to form two domains, the first having a core parallel sheet flanked on one side by at least two helices and on the other by an antiparallel amphiphilic sheet, with an additional helix connecting the two sheets. The second domain is built entirely from b strands. Proteins 27:279-289
π SIMILAR VOLUMES
## Abstract To investigate the role of the Nβterminal region in the lytic mechanism of the poreβforming toxin sticholysin II (St II), we studied the conformational and functional properties of peptides encompassing the first 30 residues of the protein. Peptides containing residues 1β30 (P1β30) and
The multifunctional transcription factor YY1 is associated with the nuclear matrix. In osteoblasts, the interaction of several nuclear matrix-associated transcription factors with the bone specific osteocalcin gene contributes to tissue-specific and steroid hormone-mediated transcription. A canonica