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What role do hydrogen bonds between the polypeptide backbone play in determining the overall protein structure?
Hydrogen bonds between the polypeptide backbone help stabilize the secondary and tertiary structures of proteins by forming interactions between amino acid residues. These bonds contribute to the folding and shape of the protein, ultimately determining its overall structure and function.
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Differentiate between secondary and tertiary structure by describing the parts of the polypeptide chain that participates in the bonds that hold together each level of structure?
Secondary structure refers to local folding patterns involving hydrogen bonding between the peptide backbone, forming alpha helices or beta sheets. Tertiary structure involves the overall 3D folding of the entire polypeptide chain, with interactions between side chains such as hydrophobic interactions, hydrogen bonding, disulfide bridges, and electrostatic interactions playing a major role in maintaining the structure.
A pleated sheet organization in a polypeptide chain is an example of which structure?
A pleated sheet organization in a polypeptide chain is an example of secondary protein structure, specifically beta sheet secondary structure. It involves hydrogen bonding between neighboring polypeptide strands running in opposite directions.
What aspect of protein structure are stabilized or assisted by hydrogen bonds?
secondary, tertiary, and quaternary structures, but not primary structure
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
What level of protein structure characterized by coils and folds results from hydrogen bonding between carboxyl and amino groups of the polypeptide chain?
The secondary structure of proteins, such as alpha helices and beta sheets, is characterized by coils and folds resulting from hydrogen bonding between the carboxyl and amino groups of the polypeptide chain. This stabilizes the repeating patterns of hydrogen bonds along the backbone of the protein.
The backbone of a polypeptide could be represented by?
The backbone of a polypeptide could be represented by a chain of nitrogen and hydrogen atoms. The polypeptide backbone is the key contributor to protein secondary structure, which involves backbone-to-backbone hydrogen bonding.
The coiling of the protein chain backbone into an alpha helix is referred to as?
The coiling of the protein chain backbone into an alpha helix is referred to as secondary structure. This repetitive structure is stabilized by hydrogen bonds between the backbone amide hydrogen and carbonyl oxygen atoms.
What structure describes the alpha-helices and beta-sheets that are formed by hydrogen bonding vetween backbone atoms located near each other in the polypeptide chain?
This bonding is done in the secondary structure of the protein.
Betta pleated sheets are characterized by?
folds stabilized by hydrogen bonds between segments of the polypeptide backbone.
Some regions of a polypeptide may coil or fold back on themselves?
Yes, certain regions of a polypeptide chain can coil or fold back on themselves due to interactions between amino acids within the chain. These interactions, such as hydrogen bonding and hydrophobic interactions, help stabilize the folded structure of the protein, ultimately determining its function.
Which primarily responsible for the helical structure of a polypeptide chain?
The primary structure of a polypeptide chain, consisting of a sequence of amino acids, is primarily responsible for the helical structure of a polypeptide chain. In particular, the recurring hydrogen bonding between the carbonyl oxygen of one residue and the amide hydrogen of another residue stabilizes the helical conformation, leading to the formation of an alpha helix.
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.
Differentiate between secondary and tertiary structure by describing the parts of the polypeptide chain that participates in the bonds that hold together each level of structure?
Secondary structure refers to local folding patterns involving hydrogen bonding between the peptide backbone, forming alpha helices or beta sheets. Tertiary structure involves the overall 3D folding of the entire polypeptide chain, with interactions between side chains such as hydrophobic interactions, hydrogen bonding, disulfide bridges, and electrostatic interactions playing a major role in maintaining the structure.
A pleated sheet organization in a polypeptide chain is an example of which structure?
A pleated sheet organization in a polypeptide chain is an example of secondary protein structure, specifically beta sheet secondary structure. It involves hydrogen bonding between neighboring polypeptide strands running in opposite directions.
What aspect of protein structure are stabilized or assisted by hydrogen bonds?
secondary, tertiary, and quaternary structures, but not primary structure
What are the forces which create the tertiary structure of a polypeptide?
The tertiary structure of a polypeptide is primarily determined by interactions between the R-groups of amino acids in the protein. These interactions include hydrogen bonding, disulfide bonds, hydrophobic interactions, and electrostatic interactions. The overall folding of the polypeptide chain into its tertiary structure is crucial for the protein's function.
Hydrogen bonds between different parts of the polypeptide chain result in which level of protein structure?
Hydrogen bonds between different parts of the polypeptide chain contribute to the secondary structure of proteins, specifically in the formation of alpha helices and beta sheets. These secondary structures then further fold and interact to form the tertiary structure of the protein.
