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

Publication Type:

Journal Article

Authors:

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

Source:

Volume 12, Issue 2, p.123 - 137 (2005)

URL:

PM:15723638

Keywords:

Antigens; Bacterial; chemistry; genetics; metabolism; Bacterial Proteins; Binding Sites; Enzyme Stability; Histidine; Hydrogen Bonding; Models; Molecular; Phosphoenolpyruvate Sugar Phosphotransferase System; Protein Conformation; Protein Denaturation; Prote

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

Notes:

DA - 20050222
IS - 0929-8665 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Antigens, Bacterial)
RN - 0 (Bacterial Proteins)
RN - 56-45-1 (Serine)
RN - 71-00-1 (Histidine)
RN - EC 2.7.1.- (Phosphoenolpyruvate Sugar Phosphotransferase System)
RN - EC 2.7.1.- (phosphocarrier protein HPr)
SB - IM