Question

The terms motif (fold) and domain describe levels of protein organization more complicated than primary or secondary structure. Differentiate between motifs and domains by matching each phrase to the appropriate term. Motifs Domains Both Answer Bank clusters of secondary structure may retain a three-dimensional structure when separated from the rest of the protein Baß unit stable, globular units unit of tertiary structure depends on primary structure may be distinct functional units in a protein stabilized by hydrophobic interactions repetitive supersecondary structure

Answer 1

Motifs 1. repetitive super secondary structure 2. Baßunit Domains 1. Stable, globular units 2. may retain a three- dimensional structure when separated from the rest of the protein 3. may be distinct functional units in a protein Both 1. Stabilized by hydrophobic interactions 2. units of tertiary structure 3. depends on primary structure 3.clusters of secondary structure The protein is formed by the small blocks of amino acids hence, they are called building blocks of the protein. An amino acid is an organic molecule, it is made up of a basic amino group (at amino-terminal NI-NH2) and an acidic carboxyl group (at carboxy-terminal-COOH), along with the amino-terminal and carboxy-terminal it has an organic side chain (R-group). The R group side chain is unique for each amino acid. In a molecule, central carbon atom (alpha- carbon) is located, where both amino and carboxyl groups are attached in two sides and the other two sides of the carbon are satisfied by the R group side chain and a hydrogen atom. During the denaturation of the protein, the secondary and tertiary structures are disrupted. The disruption of the peptide bond by denaturation reactions is not an easy task, it needs a lot of strength. The sequence of amino acids in the primary structure same after a denaturation process. Denaturation results in the disruption of the secondary structure of the protein (alpha-helix and beta sheets are uncoiled in random shape). There are four types of bonding interactions in the tertiary structure of the protein, they are salt bridges, hydrogen bonding, disulfide bonds, and non-polar hydrophobic interactions. These four types of bonding interactions may get disrupted.