A chain Nterminal Gly le Vai Glu Gio Cys Cys Thr Ser lHle Cs Ser Leu Tyr Glo Leu Glu Asn Tyr Cs Aso Cterminal B chain N-terminal Phe Val Asm Gin His Leu Cys Gly Ser His Leu Val Glu Ala Leu Try Leu Vai Cs Gy Glu Ang Ghy Phe Phe T The Pro Lys Ala Gterminal FIGURE 27.16 Human insulin. The A chain of 21 amino acids and B chain of 30 amino acids are connected by interchain disulfide bonds between A7 and B7 and between A20 and B19. In addition, a single intrachain disulfide bond occurs belween Aó and Al1.
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.
Examine the amino acid sequence of human insulin (Figure 27.16) and list each Asp, Glu, His, Lys, and Arg in this molecule. Do you expect human insulin to have an
isoelectric point nearer that of the acidic amino acids (pI 2.0–3.0), the neutral amino acids (pI 5.5–6.5) or the basic amino acids (pI 9.5–11.0)?
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