In protein tertiary structure, hydrophobic interactions occur when hydrophobic amino acids, which contain only carbon and hydrogen atoms, cluster together. This clustering helps hold loops of the polypeptide backbone in place.

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The tertiary structure of a protein is the large-scale, three-dimensional shape of a single polypeptide chain. This conformation is determined by various interactions between amino acid residues that are far apart in the chain, including disulfide bridges (covalent bonds between sulfhydryl, or $$-\text{SH}$$, groups of side chains), hydrogen bonds, ionic bonds, and hydrophobic interactions.

Tertiary Structure

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Microbiology covers the scope and sequence requirements for a single-semester microbiology course for non-majors. The book presents the core concepts of microbiology with a focus on applications for careers in allied health. The pedagogical features of the text make the material interesting and accessible while maintaining the career-application focus and scientific rigor inherent in the subject matter. Microbiology’s art program enhances students’ understanding of concepts through clear and effective illustrations, diagrams, and photographs.

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Protein folding is the biological process by which a polypeptide chain assumes its large-scale, three-dimensional shape.

Protein Folding

In protein tertiary structure, an ionic bond is an attraction that occurs between a positively charged amino acid and a negatively charged amino acid. These ionic interactions work to hold loops of the polypeptide backbone in place.

Ionic Bonds in Protein Tertiary Structure

Hydrophobic Interactions in Protein Tertiary Structure

In protein tertiary structure, a disulfide linkage is a covalent bond formed when the sulfur atom of one amino acid binds to the sulfur atom of another. This linkage helps hold loops of the polypeptide backbone in place.

Disulfide Linkages in Protein Tertiary Structure

In protein tertiary structure, a hydrogen bond is an attraction between two polar amino acids. These attractions help hold loops of the polypeptide backbone in place.

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