Covalent inhibitors of cooperativity in hemoglobin. 1972

W Konigsberg, and S Simon, and D J Arndt, and K Moffat

UI MeSH Term Description Entries
D008301 Maleimides Derivatives of maleimide (the structural formula H2C2(CO)2NH) containing a pyrroledione ring where the hydrogen atom of the NH group is replaced with aliphatic or aromatic groups.
D008961 Models, Structural A representation, generally small in scale, to show the structure, construction, or appearance of something. (From Random House Unabridged Dictionary, 2d ed) Model, Structural,Structural Model,Structural Models
D010108 Oxyhemoglobins A compound formed by the combination of hemoglobin and oxygen. It is a complex in which the oxygen is bound directly to the iron without causing a change from the ferrous to the ferric state. Oxycobalt Hemoglobin,Oxycobalthemoglobin,Oxyhemoglobin,Hemoglobin, Oxycobalt
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D001965 Bromides Salts of hydrobromic acid, HBr, with the bromine atom in the 1- oxidation state. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Bromide
D002250 Carbon Radioisotopes Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes. Radioisotopes, Carbon
D006454 Hemoglobins The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements. Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
D006736 Horses Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest. Equus caballus,Equus przewalskii,Horse, Domestic,Domestic Horse,Domestic Horses,Horse,Horses, Domestic
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013237 Stereoisomerism The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed) Molecular Stereochemistry,Stereoisomers,Stereochemistry, Molecular,Stereoisomer

Related Publications

W Konigsberg, and S Simon, and D J Arndt, and K Moffat
January 2018, Current protein & peptide science,
W Konigsberg, and S Simon, and D J Arndt, and K Moffat
May 1975, Biochemistry,
W Konigsberg, and S Simon, and D J Arndt, and K Moffat
May 1987, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
W Konigsberg, and S Simon, and D J Arndt, and K Moffat
May 1987, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
W Konigsberg, and S Simon, and D J Arndt, and K Moffat
May 1987, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
W Konigsberg, and S Simon, and D J Arndt, and K Moffat
January 2004, Methods in enzymology,
W Konigsberg, and S Simon, and D J Arndt, and K Moffat
January 1992, Science (New York, N.Y.),
W Konigsberg, and S Simon, and D J Arndt, and K Moffat
December 1973, Annals of the New York Academy of Sciences,
W Konigsberg, and S Simon, and D J Arndt, and K Moffat
January 1974, Molecular biology, biochemistry, and biophysics,
W Konigsberg, and S Simon, and D J Arndt, and K Moffat
December 1973, Biophysical chemistry,
Copied contents to your clipboard!