Look at the protein below. Label the diagram on the right and show which part of the protein had hydrophobic amino acid residues and what part of the protein has hydrophilic amino acid residues. Explain how you know.

Respuesta :

The tertiary structure of proteins provides them with a more stable shape. The hydrophilic amino acids remain on the surface of the folded protein, while the hydrophobic ones stay in the center of the molecule, isolated from water.

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Proteins are amino acid polymers linearly arranged and connected by peptidic bonds. These molecules characterize by their different structures.  

Amino acids are organic molecules composed of

  • a central carbon,
  • one hydrogen atom,
  • one carboxyl group,
  • one amine group, and
  • one R group.

The composition of the R group is what makes them different from each other.

Twenty amino acids compose the different proteins. Some of them are non-polar.

When amino acids are non-polar, their R-groups are not stable in contact with water, meaning that non-polar amino acids are hydrophobic. Their lateral chains have almost entirely C-C and C-H bonds. These amino acids are alanine, valine, leucine, isoleucine, methionine, tyrosine, phenylalanine, tryptophan.

The hydrophilic amino acids can associate with water. Among them, we can find arginine, glycine, glutamine, asparagine, histidine, aspartic acid, glutamic acid.

When proteins are synthesized, they acquire a three-dimensional structure that makes them more stable.

Lineal polypeptides get folded and, by different types of bonds, they acquire a shape that makes them more stable.

The tertiary structure makes them capable of accomplishing their biological roles.

In an aqueous environment, the folded molecule exhibits its hydrophilic R-groups on the surface in contact with water while its hydrophobic groups remain in the structure interior.

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