Hydrogen bonding may occur between amine and carbonyl functional groups within the peptide backbone (excluding the R side group), resulting in localized folding of the polypeptide chain into helices and sheets.

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The size (length) and specific amino acid sequence of a protein are major determinants of its shape, and the shape of a protein is critical to its function. Protein structure is categorized in terms of four levels:
- Primary Structure
- Secondary Structure
- Tertiary Structure
- Quaternary Structure

Protien 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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This is simply the sequence of amino acids that make up the polypeptide chain.

Primary Structure

Secondary Structure

The process by which a polypeptide chain assumes a large-scale, three-dimensional shape through protein folding. Folded proteins tend to be native in structure.

Tertiary Structure

Assemblies of several separate  protein subunits. These proteins function adequately only when all subunits are present and appropriately configured. They are usually held together by weak interactions.

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