Biochemistry, Histidine - StatPearls - NCBI Bookshelf
WEBJul 30, 2023 · Histidine is a significant catalytic residue in the enzymes of many classes of biological reactions; its efficiency at shuttling protons greatly enhances catalysis. Histidine is essential in acid-base catalysis due to its amphoteric properties.
Histidine - Wikipedia
WEBThe imidazole sidechain of the histidine residue commonly serves as a ligand in metalloproteins. One example is the axial base attached to Fe in myoglobin and hemoglobin. Poly-histidine tags (of six or more consecutive H residues) are utilized for protein purification by binding to columns with nickel or cobalt, with micromolar affinity. [12]
Histidine: A Systematic Review on Metabolism and Physiological Effects ...
WEBMay 14, 2020 · Buffering role of histidine and histidine-related compounds (HRC): Histidine and HRC have a specific role in the intracellular, non-bicarbonate buffering capacity of vertebrate muscle, which is mainly supported by the imidazole groups of free histidine or histidine residues in proteins as well as HRC, in the pH range of 6.5–7.5 (Figure 2 ...
The multiple roles of histidine in protein interactions - PMC
WEBMar 1, 2013 · Among the 20 natural amino acids histidine is the most active and versatile member that plays the multiple roles in protein interactions, often the key residue in enzyme catalytic reactions. A theoretical and comprehensive study on the structural features and interaction properties of histidine is certainly helpful.
Revisiting the pH-gated conformational switch on the ... - Nature
WEBFeb 7, 2020 · Histidine is a versatile residue playing key roles in enzyme catalysis thanks to the chemistry of its imidazole group that can serve as nucleophile, general acid or base depending on its...
Histidine in Proteins: pH-Dependent Interplay between π–π, …
WEBJul 22, 2024 · Quantifying the interaction geometry and energetics of histidine residues within proteins demands knowledge of their protonation state. However, distinguishing between neutral and charged His states is challenging due to the limitations on directly observing hydrogen atoms in X-ray structures.
Histidine Residue - an overview | ScienceDirect Topics
WEBHistidine residues, with their imidazole sidechains, invariably play critical roles in both copper and zinc coordination in proteins.
The protonation state of an evolutionarily conserved histidine ...
WEBApr 1, 2019 · In this study, we explore the impact of each histidine residue in the dimerization and folding stability of the forkhead domain of FoxP1 using both wild type protein (wt) and the H59A mutant.
The multiple roles of histidine in protein interactions
WEBMar 1, 2013 · Among the 20 natural amino acids histidine is the most active and versatile member that plays the multiple roles in protein interactions, often the key residue in enzyme catalytic reactions. A theoretical and comprehensive study on the structural features and interaction properties of histidine is certainly helpful.
Effect of histidine protonation state on ligand binding at the ATP ...
WEBJan 17, 2024 · Histidine residues contribute to numerous molecular interactions, owing to their structure with the ionizable aromatic side chain with pKa close to the physiological pH.