Title | HPr as a model protein in structure, interaction, folding and stability studies. |
Publication Type | Journal Article |
Year of Publication | 2005 |
Authors | Azuaga, A. I., J. L. Neira, and N. A. J. van Nuland |
Journal | Protein Pept Lett |
Volume | 12 |
Issue | 2 |
Pagination | 123-37 |
Date Published | 2005 Feb |
ISSN | 0929-8665 |
Keywords | Antigens, Bacterial, Bacterial Proteins, Binding Sites, Enzyme Stability, Histidine, Hydrogen Bonding, Models, Molecular, Phosphoenolpyruvate Sugar Phosphotransferase System, Protein Conformation, Protein Denaturation, Protein Folding, Serine |
Abstract | The small size and lack of disulphide bonds or cofactors in the Histidine-containing phosphocarrier protein (HPr) makes it an attractive system with which to study structure, interaction to its enzymatic partners, and its stability and folding. Here we give an overview on the immense work that has been performed on this protein and we will show that HPr has been widely used as a model protein to study important aspects in modern Structural Biology. |
Alternate Journal | Protein Pept. Lett. |
PubMed ID | 15723638 |
- Log in to post comments
- Google Scholar
- PubMed