| D009154 |
Mutation |
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. |
Mutations |
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| D009994 |
Osmolar Concentration |
The concentration of osmotically active particles in solution expressed in terms of osmoles of solute per liter of solution. Osmolality is expressed in terms of osmoles of solute per kilogram of solvent. |
Ionic Strength,Osmolality,Osmolarity,Concentration, Osmolar,Concentrations, Osmolar,Ionic Strengths,Osmolalities,Osmolar Concentrations,Osmolarities,Strength, Ionic,Strengths, Ionic |
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| D010100 |
Oxygen |
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration. |
Dioxygen,Oxygen-16,Oxygen 16 |
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| 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 |
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| D010455 |
Peptides |
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. |
Peptide,Polypeptide,Polypeptides |
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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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| D004591 |
Electrophoresis, Polyacrylamide Gel |
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. |
Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs |
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| D006451 |
Hemoglobin, Sickle |
An abnormal hemoglobin resulting from the substitution of valine for glutamic acid at position 6 of the beta chain of the globin moiety. The heterozygous state results in sickle cell trait, the homozygous in sickle cell anemia. |
Hemoglobin S,Deoxygenated Sickle Hemoglobin,Deoxyhemoglobin S,Hemoglobin SS,Hemoglobin, Deoxygenated Sickle,SS, Hemoglobin,Sickle Hemoglobin,Sickle Hemoglobin, Deoxygenated |
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| D006455 |
Hemoglobins, Abnormal |
Hemoglobins characterized by structural alterations within the molecule. The alteration can be either absence, addition or substitution of one or more amino acids in the globin part of the molecule at selected positions in the polypeptide chains. |
Abnormal Hemoglobins |
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