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

A I Azuaga; J L Neira; N A J van Nuland

doi:10.2174/0929866053005818

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

A I Azuaga·J L Neira·N A J van Nuland

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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.

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Antigens, Bacterial Bacterial Proteins Binding Sites Enzyme Stability Histidine Hydrogen Bonding Models, Molecular Phosphoenolpyruvate Sugar Phosphotransferase System Protein Conformation Protein Denaturation Protein Folding Serine Journal Article Research Support, Non-U.S. Gov't

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A I Azuaga, J L Neira, N A J van Nuland. 2005. HPr as a model protein in structure, interaction, folding and stability studies.. https://doi.org/10.2174/0929866053005818

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