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

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.

Keywords: hpr, pts, protein structure, protein-protein interaction, stability, folding

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Protein & Peptide Letters

Title: HPr as a Model Protein in Structure, Interaction, Folding and Stability Studies

Volume: 12 Issue: 2

Author(s): A. I. Azuaga, J. L. Neira and N. A.J. van Nuland

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Keywords: hpr, pts, protein structure, protein-protein interaction, stability, folding

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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Azuaga I. A., Neira L. J. and Nuland A.J. van N., HPr as a Model Protein in Structure, Interaction, Folding and Stability Studies, Protein & Peptide Letters 2005; 12 (2) . https://dx.doi.org/10.2174/0929866053005818