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secondary structure of a protein
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∙ 12y ago
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The alpha helix and beta pleated sheet represent which level of 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
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 type of interaction stabilizes the secondary structure of a protein causing it to form an alpha-helix?
In an α-helix, the polypeptide backbone forms a repeating helical structure that is stabilized by hydrogen bonds between a carbonyl oxygen and an amine hydrogen. These hydrogen bonds occur at regular intervals of one hydrogen bond every fourth amino acid and cause the polypeptide backbone to form a helix.
What are proteins secondary structures?
Unlike the primary structure, the secondary structure is defined as the local conformation of the protein's backbone. Protein secondary structures are grouped in three major types: helices (being the most common the alpha helices), pleated sheets (also called beta structures), and turns.The combination of these three kind of secondary structures give a wide variety of forms of the protein molecules. These combinations are named supersecondary structures or motifs and occur in many unrelated globular proteins. As examples of motifs found in protein structures are: a) the beta-alpha-beta motif, the most common supersecondary structure (consists in a right-handed cross-over connection between two consecutive parallel strands of a beta sheet by an alpha helix); b) the beta hairpin motif, that consists of an antiparallel beta sheet formed by sequential segments of polypeptide chain that are connected by relatively tight reverse turns; c) the alpha-alpha motif, two successive antiparallel alpha helices pack each other with their axes inclined (one common protein with this structure is the alpha keratin); and d) the beta barrels, that are extended beta sheets that often roll up.
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 levels of protein folding would include shapes identified as helix and pleated sheet?
This is the secondary folding phase where hydrogen bonds between the side chains give you the alpha helix and the beta pleated sheet.
What can form a structure such as a helix or a sheet?
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.
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.
Name two types of secondary protein structure Explain the role of hydrogen bonds in maintaining secondary structure?
alpha Helix and Beta pleated sheet
The alpha helix and beta pleated sheet represent which level of 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
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 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.
Secondary protein structure?
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
Do amino acids contain alpha and beta pleated sheet in their secondary structure?
Yes, they do. Side group hydrogen bonding.
What is an alpha helix?
Hi, The DNA Helix is simply another name for DNA, and such name is used because DNA is in a double helix shape. The DNA is what determines who you are and therefore is found in every cell in our body. It is the genetic information of a human being and it contains genes, which are what determines our traits. For example, there are genes that control eye color, hair color, size of body...etc.
