IndexMeritQuaternary structureDistinctionThe primary structure of a protein refers to the sequence of amino acids within the peptide chain. the first structure is maintained by peptide bonds that are created during the protein biosynthesis process. the first structure of a protein is decided by the protein-like gene. a particular sequence of DNA nucleotides is transcribed into mRNA, which is read by the ribosome during a method known as translation. The sequence of a protein is unique to that protein and defines the structure and function of the protein. The sequence of a protein will be determined by methods such as mass spectrometry. Often, however, it is read directly from the gene sequence using the genetic code. amino acid residues are important because when a peptide bond is formed, a water molecule is lost and thus proteins are created from amino acid residues. Say no to plagiarism. Get a tailor-made essay on "Why Violent Video Games Shouldn't Be Banned"? Get an Original Essay Secondary structure refers to the pleated structures that form within a polypeptide due to interactions between the backbone atoms. (The backbone simply refers to the polypeptide chain except for the R groups.) The most common forms of secondary structures are the helix and also the folded sheet ß. Each structure is held in place by hydrogen bonds, which form between the carbonyl O of an amino acid and also the amino H. In an a helix, the carbonyl (C=O) of an amino acid is hydrogen bonded to the amino H (NH) of an amino acid. (The carbonyl of amino acid one would form a hydrogen bond with the NH of amino acid five.) This bonding pattern pulls the polypeptide chain into a helical structure that resembles a curled ribbon. The R groups of the amino acids protrude outward from the a helix, wherever they are free to move. in a ß-folded sheet, two or more segments of a polypeptide chain align next to each other, forming a sheet-like structure held together by hydrogen bonds. Hydrogen bonds form between the carbonyl and amino groups of the backbone, while the R groups extend above and below the plane of the sheet. Merit The overall three-dimensional structure of a polypeptide is called the tertiary structure. The tertiary structure is mainly the result of interactions between the R groups of the amino acids that make up the protein. R-group interactions that contribute to tertiary structure include hydrogen bonding, ionic bonding, dipole-dipole interactions, and dispersion forces. for example, R groups with similar charges will repel each other, while those with opposite charges will form an associated electrostatic bond. Polar R teams will typify gaseous bonds and alternative dipole-dipole interactions. Tertiary structures are hydrophobic interactions, during which amino acids with nonpolar hydrophobic R groups form together inside the protein, leaving the hydrophilic amino acids on the outside to act with surrounding water molecules. Quaternary Structure Many proteins are created from a polypeptide chain and have only three levels of. However, some proteins are created from multiple polypeptide chains, also called subunits. once these subunits come together, they provide the protein with its quaternary structure. Hemoglobin contains a quaternary structure. hemoglobin transports oxygen in the blood and is made up of four subunits, two each of the a type and two ß. Another example is DNA polymerase, an enzyme that synthesizes new strands of DNA and is made up of 10 subunits. In general, similar types of interactions contributing to tertiary structure (mostly interactions.