The coiling of the protein chain backbone into an alpha helix is referred to as the secondary structure. It is composed of several polypeptide chains.
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 main difference between a right-handed alpha helix and a left-handed alpha helix in protein structures is the direction in which the helix twists. In a right-handed alpha helix, the helix twists in a clockwise direction, while in a left-handed alpha helix, the helix twists in a counterclockwise direction. This difference in twisting direction affects the overall shape and stability of the protein structure.
The protein structure contains both alpha helices and beta sheets, which are the two main elements of protein secondary structure.
The alpha chain and beta chain in a protein complex differ in their structure and function. The alpha chain typically forms the core of the protein complex, providing stability and structural support. In contrast, the beta chain often plays a role in binding other molecules or ions, contributing to the overall function of the complex. These differences in structure and function allow the alpha and beta chains to work together to perform specific tasks within the protein complex.
A backbone molecule is the unchanging part of a molecule, which are linked together in a chain-like fashon. For example: An amino acid molecule consists of an amino group (usually featured on the left hand side), and a carboxyl group (usually featured on the right hand side) bound to a central (alpha) carbon atom. That is the basic (non-changing) part of the amino acid. However, to the central (alpha) carbon there is a Hydrogen atom, and a side chain (or function group) are attached (bound). That side chain is different for every amino acid, thus giving a unique property to each and every one of them. These amino acid molecules are linked together by peptide bonds, leading to the formation of a protein molecule. Since the the basic molecule parts (amino group, alpha carbon, carboxyl group) are linked to each other, forming a chain, that is what is considered as the "protein backbone". Similarly, other molecules can form a "backbone" . Other examples are: sugar-phosphate backbone in DNA, carbohydrate backbones in polysaccharide. More info can be found under related links
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.
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.
Secondary structure. The coiling is the formation of the alpha helix. The folding is the formation of the beta sheets.
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.
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 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.
This bonding is done in the secondary structure of the protein.
Alpha keratin is a protein present in hair,wool,nails, horns,hooves of mammals
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.
Mainly hydrogen bonds between the backbone amide and carbonyl groups. Other bonds, such as disulfide bonds, may also contribute to stabilizing secondary protein structures like alpha-helices and beta-sheets.
The secondary structure of protein:the ordered 3-d arrangements in localized area of a polypeptide chaininteractions of the peptide backbone (s-trans and planar)example of secondary structure : alpha-helix and beta-pleated sheet
Hydrogen bonds between the carbonyl oxygen of one amino acid and the amine hydrogen of an amino acid that is four residues down the sequence stabilize the formation of an alpha-helix in a protein. This creates a helical backbone structure that provides stability to the protein's secondary structure.