Which of these amino acid side chains would be effective at carrying out covalent catalysis in an enzyme-catalyzed reaction at pH 7.4? Assume that if more than 10% of the side chain can act as a strong nucleophile, then there will be a sufficient amount of nucleophile available for the enzyme to perform covalent catalysis. Please select all possible answers. Lysine side chain with pKa = 9.0, where the positively charged state is destabilized by a nearby arginine side chain Glutamate side chain with pKa = 6.5, where the negatively charged state is destabilized due to the presence of a nearby Asp de chain Histidine side chain with pKa = 5.5, where the positively charged state is stabilized due to the presence of a nearby Asp side chain Alanine side chain
Neutral Amino Acids
Amino acids which do not have any charge on them are neutral amino acids.
Globular Protein
The globular proteins refer to the shape of protein specifically spherical in nature apart from spherical form fibrous, disordered and membrane-bound proteins exist. These globular proteins are miscible in water and form a colloidal solution rather than other types which might not exhibit solubility. Many classes of the fold are found in globular proteins, which render them a sphere shape. Globular fold containing proteins usually are referred to by the term globin.
Dimer
Dimers are basic organic compounds, which are derivates of oligomers. It is formed by the combination of two monomers which could potentially be strong or weak and in most cases covalent or intermolecular in nature. Identical monomers are called homodimer, the non-identical dimers are called heterodimer. The method by which dimers are formed is known as “dimerization”.
Dipeptide
A dipeptide is considered a mixture of two distinct amino acids. Since the amino acids are distinct, based on their composition, two dipeptide's isomers can be produced. Various dipeptides are biologically essential and are therefore crucial to industry.
G.293.
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