| D007700 |
Kinetics |
The rate dynamics in chemical or physical systems. |
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| D008956 |
Models, Chemical |
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment. |
Chemical Models,Chemical Model,Model, Chemical |
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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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| 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 |
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| D006859 |
Hydrogen |
The first chemical element in the periodic table with atomic symbol H, and atomic number 1. Protium (atomic weight 1) is by far the most common hydrogen isotope. Hydrogen also exists as the stable isotope DEUTERIUM (atomic weight 2) and the radioactive isotope TRITIUM (atomic weight 3). Hydrogen forms into a diatomic molecule at room temperature and appears as a highly flammable colorless and odorless gas. |
Protium,Hydrogen-1 |
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| D014360 |
Trypsin Inhibitor, Kunitz Soybean |
A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin. |
Kunitz Soybean Trypsin Inhibitor,Trypsin Inhibitor DE-3,Trypsin Inhibitor Kunitz Soybean,Trypsin Inhibitor DE 3 |
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