Table of ContentsMeritQuaternary 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 created throughout the process of protein biosynthesis. The first structure of a protein is determined by the gene similar to the protein. a particular sequence of nucleotides in DNA is transcribed into mRNA, which is read by the ribosome in 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. However, it is often read directly from the gene sequence using the genetic code. Amino acid residues are important because when a peptide bond is made, 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 should not be banned”?Get original essaySecondary structure refers to the pleated structures that form within a polypeptide due to interactions between the atoms in the column vertebral. (Backbone simply refers to the polypeptide chain except for the R groups). The most common forms of secondary structures are the α-helix and also the β-folded sheet. Each structure is held in its place by hydrogen bonds, which form between the carbonyl O of an amino acid and also the amino H. In a helix, the carbonyl (C=O) of an amino acid is linked by hydrogen to 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 coiled ribbon. The R groups of amino acids exit the α-helix wherever they are free to move. In a β-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 backbone carbonyl and amino groups, while the R groups extend above and below the plane of the sheet. Merit The overall three-dimensional structure of a polypeptide is called its tertiary structure. The tertiary structure results mainly from 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 repel each other, while those with opposite charges will associate with electrostatic bonding. Polar R teams will explore gas bonds and alternative dipole-dipole interactions. Tertiary structures are hydrophobic interactions, in which amino acids with nonpolar and hydrophobic R groups form together inside the protein, leaving the hydrophilic amino acids outside to act with water molecules surrounding areas. 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 give the protein its quaternary structure. Hemoglobin contains a quaternary structure. Hemoglobin carries oxygen in the blood and is made up of four subunits, two of each type.