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.
secondary structure of a protein
The alpha helix and beta sheets are found at the Secondary level of protein folding. It's when the protein is taking its shape. Secondary structure
Yes, they do. Side group hydrogen bonding.
'The Quaternary structure of a protein is the 4th level of folding for a protein. An example of this would be a red blood cell, which is a quaternary structure, it is made up of alpha helicies and also beta pleated in the tertiary structure. The Quaternary structure of a protein contains 4 tertiary structures in it.
Proteins have primary structure, which is their amino acid sequence, secondary structure, which is either the alpha helix or the beta pleated sheet, tertiary structure, the protein's geometric shape, and quaternary structure, the arrangement of multiple protein subunits.
secondary structure of a protein
secondary structure
together they make a secondary protein structure
The alpha helix and beta sheets are found at the Secondary level of protein folding. It's when the protein is taking its shape. Secondary 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.
alpha Helix and Beta pleated sheet
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.
A polypeptide chain, which is the primary structure of a protein, can fold into secondary structures such as an alpha-helix or a beta-sheet.
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 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.
While it is possible to predict likely secondary structures of a protein from its primary structure, only knowing the secondary structure, the general 3-D shape of local areas of the protein, cannot yield the primary structure.