1. Three dimensional relationship of the different polypeptide chains in a multisubunit protein or protein complex K. Quaternary structure
2. Common folding pattern in proteins in which a linear sequence of amino acids folds into a right-handed coil stabilized by internal hydrogen-bonding between polypeptide backbone atoms. J. Alpha-helix
3. The amino acid sequence of a protein A. Primary structure
4. A region on the surface of a protein that can interact with another molecule through noncovalent bonding. I. Binding site
5. Three-dimensional arrangement of alpha-helices and beta-sheets within a single polypeptide, typically stabilized by a variety of noncovalent bonds, including ionic and hydrogen bonds, and nonpolar interactions / hydrophobic force. H. Tertiary structure
6. The chain of repeating carbon and nitrogen atoms, linked by peptide bonds, in a protein. E. Polypeptide backbone
7. Common structural motif in proteins in which different sections of the polypeptide chain run alongside each other and are joined together by hydrogen bonding between atoms of the polypeptide backbone. B. Beta-sheet
8. Portion of a polypeptide chain that has a discrete tertiary structure of its own and can often fold independently of the rest of the chain L. Protein domain
9. Regular local folding patterns in a protein, including alpha-helix and beta-sheet F. Secondary structure
C. Protein - large macromolecules composed of one or more long chains of amino acid residues with various functions within the cell.
D. Coiled-coil - a structural motif in proteins in which alpha-helices are coiled together (like a rope)
G. Side chain - a chemical group that is attached to a backbone.
