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The alpha helix and beta pleated sheet represent which level of protein structure?
The alpha helix and beta pleated sheet represent the secondary structure of proteins. Both structures are formed by the interaction of amino acids within the polypeptide chain through hydrogen bonding.
What level of protein structure is associated the alpha helix and beta pleated sheet?
It depends on the primary sequence of amino acids as to which secondary structure is more stable. Both structures use hydrogen bonds to stabilize the structures, however in an alpha helix, these hydrogen bonds are with the peptide and in beta sheets the hydrogen bonds are between beta peptide strands. I really don't know which structure is more stable... -alpha helix seems to be a more common structure -and B sheets lose some H bonding during hair pin turns and during twists. -But an alpha helix has a dipole whereas an antiparalle beta sheet doesnt. -weighing it up i would assume an alpha helix to be more stable but that would be a guess from me.
Do amino acids contain alpha and beta pleated sheet in their secondary structure?
Yes, they do. Side group hydrogen bonding.
What do you call the 2 types of secondary protein structure which are evident in a polypeptide cha in?
The two types of secondary protein structure are alpha helix and beta sheet. In an alpha helix, the polypeptide chain is tightly coiled in a helical shape, while in a beta sheet, the polypeptide chain is folded into a sheet-like structure with hydrogen bonds between neighboring strands.
What type of interaction stabilizes the secondary structure of a protein causing it to form an alpha-helix?
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.
Structure of keratin?
Alpha keratin has alpha helix structure and beta keratin has beta pleated sheet structure.
What type of protein shape is characterized by the alpha helix or a flat-pleated sheet?
secondary structure
What are the two most common secondary structures in a protein?
The two types of tertiary protein structures: globular and fibrous proteins. Globular proteins act as enzymes that catalyze chemical reactions in organisms. Fibrous proteins like collagen play structural role.
The alpha helix and beta pleated sheet represent which level of protein structure?
The alpha helix and beta pleated sheet represent the secondary structure of proteins. Both structures are formed by the interaction of amino acids within the polypeptide chain through hydrogen bonding.
Is it aminoaacids that are the secondary structure of alpha helix and beta pleated?
The secondary structures of alpha helix and beta pleated sheets are formed by hydrogen bonding between amino acids in a protein chain. In an alpha helix, the hydrogen bonding occurs between amino acids in the same chain, leading to a helical structure. In beta pleated sheets, hydrogen bonding occurs between amino acids in different segments of the protein chain, creating a sheet-like structure.
What levels of protein folding would include shapes identified as helix and pleated sheet?
The secondary level of protein folding includes the formation of alpha helices and beta sheets, which are common in protein structures. These structures result from hydrogen bonding between amino acids in the protein chain, leading to the characteristic helical or sheet-like shapes.
Which type of interaction stabilizes the alpha helix and the beta pleated sheets of a protein?
Hydrogen bonding is the primary interaction that stabilizes the alpha helix and beta pleated sheets of a protein. In the case of alpha helices, hydrogen bonds form between the carbonyl oxygen of one amino acid residue and the amide hydrogen of another residue in the chain. In beta sheets, hydrogen bonds form between adjacent strands of the sheet.
Do the coils and folds of a protein's amino acid chain make up the protein's primary structure?
The coils of an alpha helix or the folds of a beta-pleated sheet are a characteristic of the secondary structure.
What can form a structure such as a helix or a sheet?
Proteins can form structures such as a helix or a sheet due to the specific arrangement of amino acids in their sequence. The hydrogen bonding between the amino acids in the polypeptide chain determines the secondary structure of the protein, leading to the formation of helices and sheets.
Name two types of secondary protein structure Explain the role of hydrogen bonds in maintaining secondary structure?
Two types of secondary protein structure are alpha helix and beta sheet. Hydrogen bonds play a crucial role in maintaining these structures by forming between the carbonyl oxygen of one amino acid and the amide hydrogen of another, stabilizing the repeating patterns of amino acids in the helix or sheet. This helps in maintaining the overall shape and stability of the protein.
What level of protein structure is associated the alpha helix and beta pleated sheet?
It depends on the primary sequence of amino acids as to which secondary structure is more stable. Both structures use hydrogen bonds to stabilize the structures, however in an alpha helix, these hydrogen bonds are with the peptide and in beta sheets the hydrogen bonds are between beta peptide strands. I really don't know which structure is more stable... -alpha helix seems to be a more common structure -and B sheets lose some H bonding during hair pin turns and during twists. -But an alpha helix has a dipole whereas an antiparalle beta sheet doesnt. -weighing it up i would assume an alpha helix to be more stable but that would be a guess from me.
Do amino acids contain alpha and beta pleated sheet in their secondary structure?
Yes, they do. Side group hydrogen bonding.
