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Three-fold structural pattern in the soybean trypsin inhibitor (Kunitz). 1979

A D McLachlan

UI MeSH Term Description Entries
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
D006860 Hydrogen Bonding A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds. Hydrogen Bonds,Bond, Hydrogen,Hydrogen Bond
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
D014361 Trypsin Inhibitors Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds. Trypsin Inhibitor,Inhibitor, Trypsin,Inhibitors, Trypsin

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