Homeodomains are a class of helix-turn-helix DNA-binding protein motifs that play an important role in the control of cellular development in eukaryotes. They fold in a three β£-helix structural module, where the third helix is the recognition helix that fits into the major groove of DNA. Structural
Structural and functional role of nickel ions in urease by molecular dynamics simulation
β Scribed by Jing Lv; Yongjun Jiang; Qingsen Yu; Shaoyong Lu
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 1015 KB
- Volume
- 16
- Category
- Article
- ISSN
- 1432-1327
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π SIMILAR VOLUMES
relationships between the structural features of the Ni-containing active site and the physico-chemical and biochemical properties of this metallo-enzyme. In addition, the recently determined structure of a complex between urease and a transition state analogue is discussed as it leads to a novel, t
Isolated (SFs)5s clusters, as studied by computer simulation, exhibit a phase behavior which is essentially similar to the bulk material. Conversely, the molecular packing of (SF6)ts is close-to-icosahedral. No sign of a transition with coexistence of rigid and non-rigid states was found in (SF,) ,x