NMR structure of the C-terminal domain of SecA in the free state
β Scribed by William M. Matousek; Andrei T. Alexandrescu
- Publisher
- Elsevier Science
- Year
- 2004
- Tongue
- English
- Weight
- 680 KB
- Volume
- 1702
- Category
- Article
- ISSN
- 1570-9639
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The structure of the C-terminal DNA-binding domain of human immunovirus-1 integrase has been refined using nuclear magnetic resonance spectroscopy. The protein is a dimer in solution and shows a well-defined dimer interface. The folding topology of the monomer consists of a fivestranded β€-barrel tha
Mouse capping enzyme (Mce1) consists of two functional domains: the amino-terminal triphosphatase domain and the carboxyl-terminal guanylyltransferase (GTase) domain. The bifunctional Mce1 gene encodes 597 a.a. with a molecular weight approximately 68 kDa. Mce1 cDNA is located on chromosome 4A4 appr
A variety of nmr transient techniques demonstrate the absence of domain structures in powders of a-and /3-cyclodextrins, dextran B512F, and their "deuterated" analogs where deuterium replaces exchangeable protons. Cyclodextrins and dextran are inferred to be homogeneously ordered and disordered one-
Hepatitis C virus (HCV) is a human pathogen affecting nearly 3% of the world's population. Chronic infections can lead to cirrhosis and liver cancer. The RNA replication machine of HCV is a multi-subunit membrane-associated complex. The nonstructural protein NS5A is an active component of HCV replic