| D008970 |
Molecular Weight |
The sum of the weight of all the atoms in a molecule. |
Molecular Weights,Weight, Molecular,Weights, Molecular |
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| D009218 |
Myosins |
A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. |
Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase |
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| D009751 |
Nutritional Requirements |
The amounts of various substances in food needed by an organism to sustain healthy life. |
Dietary Requirements,Nutrition Requirements,Dietary Requirement,Nutrition Requirement,Nutritional Requirement,Requirement, Dietary,Requirement, Nutrition,Requirement, Nutritional,Requirements, Dietary,Requirements, Nutrition,Requirements, Nutritional |
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| D010288 |
Parenteral Nutrition |
The administering of nutrients for assimilation and utilization by a patient who cannot maintain adequate nutrition by enteral feeding alone. Nutrients are administered by a route other than the alimentary canal (e.g., intravenously, subcutaneously). |
Intravenous Feeding,Nutrition, Parenteral,Parenteral Feeding,Feeding, Intravenous,Feeding, Parenteral,Feedings, Intravenous,Feedings, Parenteral,Intravenous Feedings,Parenteral Feedings |
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| D011506 |
Proteins |
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. |
Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene |
|
| D002149 |
Energy Intake |
Total number of calories taken in daily whether ingested or by parenteral routes. |
Caloric Intake,Calorie Intake,Intake, Calorie,Intake, Energy |
|
| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
|
| D000199 |
Actins |
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle. |
F-Actin,G-Actin,Actin,Isoactin,N-Actin,alpha-Actin,alpha-Isoactin,beta-Actin,gamma-Actin,F Actin,G Actin,N Actin,alpha Actin,alpha Isoactin,beta Actin,gamma Actin |
|
| D000418 |
Albumins |
Water-soluble proteins found in egg whites, blood, lymph, and other tissues and fluids. They coagulate upon heating. |
Albumin |
|
| D000601 |
Amino Acids, Essential |
Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs. |
Essential Amino Acid,Essential Amino Acids,Acid, Essential Amino,Acids, Essential Amino,Amino Acid, Essential |
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