Kurt Wuethrich, the ETH Zuerich, and the Development of NMR Spectroscopy for the Investigation of Structure, Dynamics, and Folding of Proteins
✍ Scribed by Harald Schwalbe
- Publisher
- John Wiley and Sons
- Year
- 2003
- Weight
- 75 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0931-7597
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Mastoparan‐X, a 14‐residue peptide found in wasp venom, does not adopt a well‐defined structure in water, but it folds into an α‐helix upon addition of trifluoroethanol (TFE). At low levels of TFE, the peptide is partially folded, passing through intermediate stages of folding as the am
The DNA-binding protein HU from Bacillus stearothermophilus (HUBst) is a dimer with a molecular weight of 195 kDa that is capable of bending DNA. An x-ray structure has been determined previously [Tanaka et al. 1984) Nature, vol. 310, pp. 376-381], but no structure could be established for a large p
An alpha/beta barrel is predicted for the three-dimensional (3D) structure of Bacillus subtilis ferrochelatase. To arrive at this structure, the THREADER program was used to find possible homologous 3D structures and to predict the secondary structure for the ferrochelatase sequence. The secondary s
The conserved residues of glutamyl tRNA reductase (GTR) from Hordeum vulgare (GTRhorvu) were found from an alignment/pile-up of 24 homologous sequences found using BLAST searches. A multiple alignment of sequences was used to obtain a prediction of the secondary structure of the GTR's. This secondar