Histidine rich protein II[edit]. The histidine-rich protein II (HRP II) is a histidine- and alanine-rich, water-soluble protein ... "Comparative analysis of the Plasmodium falciparum histidine-rich proteins HRP-I, HRP-II and HRP-III in malaria parasites of ... "Genetic diversity of Plasmodium falciparum histidine-rich protein 2 (PfHRP2) and its effect on the performance of PfHRP2-based ... "Plasmodium falciparum Histidine-Rich Protein 2-Based Immunocapture Diagnostic Assay for Malaria: Cross-Reactivity with ...
Histidine. 0.726 g. Alanine. 1.436 g. Aspartic acid. 2.200 g. Glutamic acid. 3.610 g. ...
Histidine. 0.389 g. Alanine. 0.662 g. Aspartic acid. 1.368 g. Glutamic acid. 2.885 g. ...
Histidine. 0.557 g. Alanine. 1.027 g. Aspartic acid. 2.911 g. Glutamic acid. 6.810 g. ...
Histidine. 0.255 g. Alanine. 0.509 g. Aspartic acid. 1.222 g. Glutamic acid. 2.393 g. ...
Histidine. 1.085 g. Alanine. 4.515 g. Aspartic acid. 5.793 g. Glutamic acid. 8.386 g. ...
... usually occurs on serine, threonine, tyrosine and histidine residues in eukaryotic proteins. Histidine ... and some lower eukaryotes histidine's nitrogen act as a nucleophile and binds to a phosphate group.[38] Once histidine is ... Histidine and aspartate phosphorylation occurs in prokaryotes as part of two-component signaling and in some cases in ... Recent evidence confirms widespread histidine phosphorylation at both the 1 and 3 N-atoms of the imidazole ring [6][7] Recent ...
Histidine. 0.067 g. Alanine. 0.161 g. Aspartic acid. 0.417 g. Glutamic acid. 0.312 g. ...
Histidine I Isoleucine J Leucine (L) or Isoleucine (I) K Lysine L Leucine ...
Thiolates, not thiols, attack disulfide bonds. Hence, thiol-disulfide exchange is inhibited at low pH (typically, below 8) where the protonated thiol form is favored relative to the deprotonated thiolate form. (The pKa of a typical thiol group is roughly 8.3, but can vary due to its environment.) Thiol-disulfide exchange is the principal reaction by which disulfide bonds are formed and rearranged in a protein. The rearrangement of disulfide bonds within a protein generally occurs via intra-protein thiol-disulfide exchange reactions; a thiolate group of a cysteine residue attacks one of the protein's own disulfide bonds. This process of disulfide rearrangement (known as disulfide shuffling) does not change the number of disulfide bonds within a protein, merely their location (i.e., which cysteines are bonded). Disulfide reshuffling is generally much faster than oxidation/reduction reactions, which change the number of disulfide bonds within a protein. The oxidation and reduction of protein ...
Histidine. 0.416 g. Alanine. 0.836 g. Aspartic acid. 1.550 g. Glutamic acid. 0.595 g. ...
Histidine. 0.077 g. Alanine. 0.170 g. Aspartic acid. 0.325 g. Glutamic acid. 0.761 g. ...
Histidine. 0.389 g. Alanine. 0.799 g. Aspartic acid. 1.261 g. Glutamic acid. 2.259 g. ...
A similar attenuation mechanism regulates the synthesis of histidine, phenylalanine and threonine. ...
Histidine His H MT-TH 12,138-12,206 L Isoleucine Ile I MT-TI 4,263-4,331 L ...
Histidine (≈6.1). Negative charge (pKa). *Aspartic acid (≈3.9). *Glutamic acid (≈4.1) ...
histidine → histamine. .mw-parser-output .nobold{font-weight:normal}. anabolism:. *Histidine decarboxylase ...
2.7.13: protein-histidine. *Protein-histidine pros-kinase. *Protein-histidine tele-kinase ...
2.7.13: protein-histidine. *Protein-histidine pros-kinase. *Protein-histidine tele-kinase ...
histidine→. *Urocanic acid. *Imidazol-4-one-5-propionic acid. *Formiminoglutamic acid. *Glutamate-1-semialdehyde ...
The iron is held in place by two histidine residues and one glutamate residue, making it a non-heme, non-iron-sulfur iron- ...
2.7.13: protein-histidine. *Protein-histidine pros-kinase. *Protein-histidine tele-kinase ...
2.7.13: protein-histidine. *Protein-histidine pros-kinase. *Protein-histidine tele-kinase ...
Histidine (≈6.1). Negative charge (pKa). *Aspartic acid (≈3.9). *Glutamic acid (≈4.1) ...
2.7.13: protein-histidine. *Protein-histidine pros-kinase. *Protein-histidine tele-kinase ...