According to the research, polar neutral and polar charged amino acids form favorable non-covalent interactions to locate in the interior of a globular protein.
It is defined as weak interactions of various origins, whether they are interactions of a dispersive nature, hydrogen bonds, dipole-dipole interactions or repulsive steric effects.
In proteins with a globular tertiary structure, the apolar side chains are oriented towards the interior of the molecule, where the most important non-covalent interactions are those of the hydrophobic type, since they require a close proximity between the apolar groups.
Therefore, we can conclude that according to the research, polar neutral and polar charged amino acids form favorable non-covalent interactions to locate in the interior of a globular protein.
Learn more about globular protein here: https://brainly.com/question/14746484
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