Secondary structure. The coiling is the formation of the alpha helix. The folding is the formation of the beta sheets.
Coiling is a common protein structure. It refers to the coiling of the polypeptide chain into an alpha-helix or a beta-sheet. Pleating is not a standard term but may refer to the folding of the protein chain into a more compact structure.
The coiling of the protein chain backbone into an alpha helix is referred to as secondary structure. This repetitive structure is stabilized by hydrogen bonds between the backbone amide hydrogen and carbonyl oxygen atoms.
The protein would have a tertiary structure. This structure results from the unique folding of the single polypeptide chain into a 3D shape, giving the protein its functional conformation.
The four levels of protein structure are differentiated from each other by the complexity of their polypeptide chain. Proteins are constructed from 20 amino acids. The levels are the hydrogen atom, a Carboxyl group, an amino group and a variable or "R" group. They have a primary structure, the order in which the amino acids are linked to form a protein. Secondary structure , coiling and folding of the polypeptide chain. Tertiary structure, is a 3-D structure of a protein chain. Quaternary is the structure of a protein macro molecule formed by interactions between several polypeptide chains..
circle Some joker listed the above as an answer to the question. The question is poorly worded, but it likely is looking for tertiary structure as an answer.
The tertiary structure is the folding
The final three-dimensional shape of any polypeptide is called its "tertiary structure." This structure results from the folding and interactions of the polypeptide chain, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. The tertiary structure is crucial for the protein's function, as it determines how the protein interacts with other molecules.
The coiling of the protein chain backbone into an alpha helix represents the secondary structure of a protein. This structure is stabilized by hydrogen bonds between the amino acid residues in the protein chain, forming a corkscrew-like structure.
The protein has a quaternary structure.In addition, each polypeptide chain has a primary, secondary, and tertiary structure.The primary structure is the sequence of amino acids in a chain.The secondary structure is the next higher level of arrangement of a chain in space, for example coiling into a alpha-helix, shaping into a beta-pleated sheet, or forming into a turn or loop.Tertiary structure is a yet higher-level folding of the chain into its final three-dimensional shape.Some proteins have only one chain, but if there are two or more, the combination of these chains to form the functional protein is the quaternary structure.
It is called secondary structure of proteins .
The tertiary structure of a polypeptide is primarily determined by interactions between the R-groups of amino acids in the protein. These interactions include hydrogen bonding, disulfide bonds, hydrophobic interactions, and electrostatic interactions. The overall folding of the polypeptide chain into its tertiary structure is crucial for the protein's function.
The coiling of the primary structure of a protein to form the helical secondary structure is due to hydrogen bonding between the amino and carboxyl groups of the amino acids in the polypeptide chain. This stable interaction creates a repeating pattern that results in the formation of an alpha-helix.