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.
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.
secondary protein structures formed by hydrogen bonds between the amino acids in a protein chain. They play a crucial role in determining the overall structure and function of proteins.
The structure of proteins that is determined by hydrogen bonds between amino acids, causing the protein to coil into helices or form pleated sheets, is known as secondary structure. This level of organization arises from the interactions between the backbone atoms in the polypeptide chain, leading to common structural motifs such as alpha helices and beta sheets. These configurations are crucial for the overall stability and function of the protein.
Yes, amylase contains both alpha helices and beta pleated sheets in its secondary structure. These structures are important for maintaining the enzyme's functional conformation and catalytic activity.
Yes, they do. Side group hydrogen bonding.
secondary structure
together they make a secondary 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.
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.
The coils of an alpha helix or the folds of a beta-pleated sheet are a characteristic of the secondary structure.
Alpha keratin has alpha helix structure and beta keratin has beta pleated sheet structure.
secondary protein structures formed by hydrogen bonds between the amino acids in a protein chain. They play a crucial role in determining the overall structure and function of proteins.
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 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
The structure of proteins that is determined by hydrogen bonds between amino acids, causing the protein to coil into helices or form pleated sheets, is known as secondary structure. This level of organization arises from the interactions between the backbone atoms in the polypeptide chain, leading to common structural motifs such as alpha helices and beta sheets. These configurations are crucial for the overall stability and function of the protein.
Yes, amylase contains both alpha helices and beta pleated sheets in its secondary structure. These structures are important for maintaining the enzyme's functional conformation and catalytic activity.
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.