HPr as a model protein in structure, interaction, folding and stability studies.

TitleHPr as a model protein in structure, interaction, folding and stability studies.
Publication TypeJournal Article
Year of Publication2005
AuthorsAzuaga, A. I., J. L. Neira, and N. A. J. van Nuland
JournalProtein Pept Lett
Volume12
Issue2
Pagination123-37
Date Published2005 Feb
ISSN0929-8665
KeywordsAntigens, 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 JournalProtein Pept. Lett.
PubMed ID15723638