The previously predicted structures of human a-lactalbumin by homology with hen egg white lysozyme by an automatic method, after the alignment stage, are compared to the X-ray determined structure of baboon a-lactalbumin. The root mean square by rotation method (RMSR) deviations for 122 C-a atoms be
A comparison of the predicted and X-ray structures of angiogenin. Implications for further studies of model building of homologous proteins
β Scribed by Simon C. Allen; K. Ravi Acharya; Kathleen A. Palmer; Robert Shapiro; Bert L. Vallee; Harold A. Scheraga
- Publisher
- Springer
- Year
- 1994
- Tongue
- English
- Weight
- 838 KB
- Volume
- 13
- Category
- Article
- ISSN
- 1573-4943
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract The homology modeling technique has been used to construct the structure of enterovirus 71 (EV 71) capsid protein VP1. The protein is consisted of 297 amino acid residues and treated as the target. The amino acid sequence identity between the target protein and sequences of template pro
13C- and 57Fe-NMR spectra of several carbon monoxide hemoprotein models with varying polar and steric effects of the distal organic superstructure, constraints of the proximal side, and solvent polarity are reported. The 13C shieldings of heme models cover a 4.0 ppm range that is extended to 7.0 ppm
The multiconformer nature of solution nuclear magnetic resonance (NMR) structures of proteins results from the effects of intramolecular dynamics, spin diffusion and an uneven distribution of structural restraints throughout the molecule. A delineation of the former from the latter two contributions