Match the descriptions / definitions with the term they best describe Three dimensional relationship of the different polypeptide chains in a multisubunit protein or protein complex Primary structure Quaternary structure Alpha-helix B 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. D. Beta-sheet Polypeptide backbone Secondary structure Protein domain Coiled-coil Protein Tertiary structure Binding site Side chain F. The amino acid sequence of a protein YA region on the surface of a protein that carn interact with another molecule through noncovalent bonding 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 L. 7The chain of repeating carbon and nitrogen atoms, linked by peptide bonds, in a protein. 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. 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 Regular local folding patterns in a protein, including alpha-helix and beta-sheet