Results 111 to 120 of about 164 (159)
Chemistry – A European Journal, Volume 31, Issue 16, March 17, 2025.The light response of CarHc protein‐based hydrogels can be alterted from photo‐weakening, to photo‐strengthening, or becoming light‐unresponsive depending on the added cofactors AdoCbl and Co2+. Under green light, CarHc tetramers disassembly weakens the hydrogel, while excess AdoCbl crosslinking poly‐histidine tags strengthens it.
Saskia Frank, Seraphine V. Wegner
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Chemistry – A European Journal, Accepted Article.Cysteine (Cys) thiolate coordination is a unique ligation motif found in heme enzymes and small molecule sensors. Divergence between these two functional classes of heme thiolate proteins is a result of distinct hydrogen bonding interactions with the axial Cys(thiolate) ligand.
Brian R. Weaver +4 more
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Chemistry – A European Journal, EarlyView.Constant pH molecular dynamics simulations are used to examine the effect of pH on amyloid‐β and its complexes with Cu(II) and Zn(II). Changes in size and secondary structure are found, with suggestions for the origin of pH‐dependent aggregation. Abstract We report the first molecular dynamics simulations to examine the effect of pH on the structure ...
Thuraya Albrahadi +2 more
wiley +1 more source
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ChemInform Abstract: INHIBITION OF HISTIDINE DECARBOXYLASE. DERIVATIVES OF HISTIDINE
Chemischer Informationsdienst, 1977AbstractAus den Nitroestern (I) entstehen mit Chlormethyl‐imidazol (II) die Substitutionsprodukte (III), die zu den Histidin‐Derivaten (IV) reduziert werden.
Helen L. White +2 more
openaire +4 more sources
Thiophosphorylation of Histidine
The Journal of Organic Chemistry, 2000The preparation of a novel phosphorus species, thiophosphoramidate, has enabled the specific thiophosphorylation of histidine at its 3-position. The rates of phosphorylation and thiophosphorylation of histidine are reported, as well as the spectroscopic properties of both thiophosphoramidate and 3-thiophosphohistidine.
Kenneth D. James +2 more
openaire +3 more sources
Science Signaling, 2001
Eukaryotic cells predominantly use serine, threonine, and tyrosine phosphorylation in various intracellular signal transduction pathways. In contrast, prokaryotic organisms employ numerous "two-component" systems, in which signaling is achieved by transferring a phosphoryl group from phosphohistidine in the "sensor kinase" component to ...
Kazuhiro Shiozaki, Jennifer L. Santos
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Eukaryotic cells predominantly use serine, threonine, and tyrosine phosphorylation in various intracellular signal transduction pathways. In contrast, prokaryotic organisms employ numerous "two-component" systems, in which signaling is achieved by transferring a phosphoryl group from phosphohistidine in the "sensor kinase" component to ...
Kazuhiro Shiozaki, Jennifer L. Santos
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DNA–histidine complex formation in isoelectric histidine buffers
Journal of Chromatography A, 1999The free solution electrophoretic mobility of two DNA molecules of different molecular masses, 18 base pairs and 2686 base pairs, has been measured in isoelectric histidine buffers with and without added low-molecular-mass electrolytes. Extensive DNA-histidine complex formation is observed in isoelectric histidine buffer, as evidenced by distortion and
Pier Giorgio Righetti +2 more
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2013
The biosynthesis of histidine has been studied extensively in Salmonella enterica and Escherichia coli. In these enterobacteria, a single operon composed of eight adjacent genes encodes the complete set of histidine biosynthetic enzymes. Three (hisD, hisNB,andhisIE) of the eight genes encode bifunctional enzymes, while two (hisH and hisF) encode a ...
P. Alifano, FANI, RENATO
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The biosynthesis of histidine has been studied extensively in Salmonella enterica and Escherichia coli. In these enterobacteria, a single operon composed of eight adjacent genes encodes the complete set of histidine biosynthetic enzymes. Three (hisD, hisNB,andhisIE) of the eight genes encode bifunctional enzymes, while two (hisH and hisF) encode a ...
P. Alifano, FANI, RENATO
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Adsorption of Histidine and Histidine-Containing Peptides on Au(111)
Langmuir, 2010The adsorption of histidine (His) and three His-derived peptides on Au(111) has been studied by soft X-ray photoelectron spectroscopy (XPS) and near-edge X-ray absorption fine structure spectroscopy (NEXAFS) at the nitrogen and oxygen K edges. The peptides were glycyl-histidine (Gly-His), glycyl-histidine-glycine (Gly-His-Gly), and glycyl-glycyl ...
Oksana Plekan +5 more
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Current Protein & Peptide Science, 2020
Protein histidine methylation is a rarely studied posttranslational modification in eukaryotes. Although the presence of N-methylhistidine was demonstrated in actin in the early 1960s, so far, only a limited number of proteins containing N-methylhistidine have been reported, including S100A9, myosin, skeletal muscle myosin light chain kinase (MLCK 2),
Sebastian Kwiatkowski, Jakub Drozak
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Protein histidine methylation is a rarely studied posttranslational modification in eukaryotes. Although the presence of N-methylhistidine was demonstrated in actin in the early 1960s, so far, only a limited number of proteins containing N-methylhistidine have been reported, including S100A9, myosin, skeletal muscle myosin light chain kinase (MLCK 2),
Sebastian Kwiatkowski, Jakub Drozak
openaire +2 more sources