HemeName: Heme Detailed information: The nonprotein portion of hemoglobin and myoglobin, consisting of reduced (ferrous) iron bound to protoporphyrin.See porphyrin hemin. Chemistry name: hem M Formula: C34H32FeN4O4 Use: Medical and biochemical research....
We describe a 1 ns molecular dynamics simulation of an 18-residue peptide (corresponding to a portion of the H helix of myoglobin) in water. The initial helical conformation progressively frays to a more disordered structure, with the lo... KV Soman,A Karimi,DA Case - 《Biopolymers》 被引...
Myoglobin has been obtained in pure crystalline form from many sources. It has amolecular weightof 16,700, about one-fourth that of hemoglobin. Though the heme portion of all myoglobins is the same, the protein portions vary considerably between species. ...
This one amino acid substitution causes a shift in the oxygen affinity curve to the left, especially at the upper portion of the curve. Thus, HbF has a higher affinity for oxygen than HbA. This allows the fetus to extract oxygen from its mother's blood in the placenta. HbF is gradually...
Other articles where heme is discussed: hemoglobin: …is made up of four heme groups surrounding a globin group, forming a tetrahedral structure. Heme, which accounts for only 4 percent of the weight of the molecule, is composed of a ringlike organic com
This invention relates to recombinant hemoglobins containing mutations in or near the heme pocket of the hemoglobin molecule. This invention particularly relates to recombinant hemoglobins that have altered geometry or polarity around the distal portion of the heme pocket....
56The distal side His32 has been shown to be attached to the most flexible portion of the polypeptide backbone in the apoprotein. The interaction between His32 and the heme is fairly strong, but during conformational changes induced by heme loading and binding to the HasR receptor, the Fe–...
It has been identified as the prosthetic group of hemoglobins, erythrocruorins (the hemoglobin analog of many invertebrates), myoglobins, some peroxidases, catalases, and cytochromes b. It is the color-furnishing portion of hemoglobin. Obtained when a soln of hematin in alkali is reduced in ...
producing decolorized hemoglobin by treating whole blood in the presence of a proteolytic enzyme at a pH of 3.5-4 to denature the globin chains and thus render the heme portion more accessible to the action of an oxidising agent. The amount of oxidising agent added to the blood is 1% by...
The fact that a significant portion of human Ab molecules interacts with heme implies that these Abs may have common molecular features of their binding sites that are suitable for the accommodation of the cofactor molecules. We hypothesize that that interaction with heme can inform for qualities of...