The coiling of the protein chain background into an alpha helix is the secondary structure. This is caused by the H-bonded arrangement of the backbone of th protein.
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 C-alpha atom is important in protein structure because it serves as a reference point for the backbone of the protein chain. It helps determine the overall shape and stability of the protein, as well as the arrangement of amino acids in the structure.
The torsion angle in protein structure is important because it determines the orientation of chemical bonds in the protein backbone. This angle affects the overall shape and stability of the protein, which in turn influences its function. By controlling the folding and flexibility of the protein, the torsion angle plays a crucial role in protein structure and function.
The structural level of a protein is most affected by disruption would be the secondary structure. It is within the secondary structure where the folding and coiling of the protein is stabilized by hydrogen bonds.
Hydrogen bonds between the polypeptide backbone help stabilize the secondary and tertiary structures of proteins by forming interactions between amino acid residues. These bonds contribute to the folding and shape of the protein, ultimately determining its overall structure and function.
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.
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.
It is called secondary structure of proteins .
Secondary structure. The coiling is the formation of the alpha helix. The folding is the formation of the beta sheets.
The backbone of a polypeptide could be represented by a chain of nitrogen and hydrogen atoms. The polypeptide backbone is the key contributor to protein secondary structure, which involves backbone-to-backbone hydrogen bonding.
All of them. Tertiary is the overall 3D shape of the protein Quaternary is what proteins it is attached to and how Primary is the actual order of the amino-acids which make up the chain Secondary is the way that that chain coils or folds So 'helix' refers to the coiling of the chain. Hence it is the secondary structure.
The C-alpha atom is important in protein structure because it serves as a reference point for the backbone of the protein chain. It helps determine the overall shape and stability of the protein, as well as the arrangement of amino acids in the structure.
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 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.
The torsion angle in protein structure is important because it determines the orientation of chemical bonds in the protein backbone. This angle affects the overall shape and stability of the protein, which in turn influences its function. By controlling the folding and flexibility of the protein, the torsion angle plays a crucial role in protein structure and function.
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..
The structural level of a protein is most affected by disruption would be the secondary structure. It is within the secondary structure where the folding and coiling of the protein is stabilized by hydrogen bonds.