| D007700 |
Kinetics |
The rate dynamics in chemical or physical systems. |
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| D008024 |
Ligands |
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed) |
Ligand |
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| D008433 |
Mathematics |
The deductive study of shape, quantity, and dependence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) |
Mathematic |
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| D009211 |
Myoglobin |
A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group. |
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| D010084 |
Oxidation-Reduction |
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). |
Redox,Oxidation Reduction |
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| D011485 |
Protein Binding |
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. |
Plasma Protein Binding Capacity,Binding, Protein |
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| 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 |
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| D002248 |
Carbon Monoxide |
Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed) |
Monoxide, Carbon |
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| D006418 |
Heme |
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins. |
Ferroprotoporphyrin,Protoheme,Haem,Heme b,Protoheme IX |
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| D006420 |
Hemeproteins |
Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480) |
Hemeprotein,Heme Protein,Heme Proteins,Protein, Heme,Proteins, Heme |
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