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Proteins with more than one polypeptide chain have what structure?
Proteins with more than one polypeptide chain have a quaternary structure. This structure is formed by the assembly of multiple polypeptide chains into a functional protein complex. The interactions between the individual polypeptide chains contribute to the overall structure and function of the protein.
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 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.
What is the significance of the interaction between serine and cysteine in protein structure and function?
The interaction between serine and cysteine in protein structure is significant because it can form disulfide bonds, which help stabilize the protein's three-dimensional structure. This interaction plays a crucial role in maintaining the protein's shape and function.
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.
Is a quaternary structure a polypeptide sequence of amino acids?
No, the polypeptide sequence of amino acids is the primary structure of a protein. The quaternary structure of the protein is the non-covalent interactions (hydrophobic binding, van der wals forces etc..) between subunits/domains of a protein.
What maintains the primary polypeptide structure?
Peptide bonds between the individual amino acids.
Proteins with more than one polypeptide chain have what structure?
Proteins with more than one polypeptide chain have a quaternary structure. This structure is formed by the assembly of multiple polypeptide chains into a functional protein complex. The interactions between the individual polypeptide chains contribute to the overall structure and function of the protein.
The structure of a protein that involves the interaction between two distinct polypeptide chains is?
Quaternary structure. This structure results from the assembly of multiple polypeptide chains to form a functional protein complex. The individual chains in the complex can interact through various types of bonds, such as hydrogen bonds, disulfide bonds, and hydrophobic interactions.
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.
Why does the primary structure of a protein coils to form the helical secondary structure?
The coiling of the primary structure of a protein to form the helical secondary structure is due to hydrogen bonding between the amino and carboxyl groups of the amino acids in the polypeptide chain. This stable interaction creates a repeating pattern that results in the formation of an alpha-helix.
What chain is a sequence of amino acids that is the foundation for the basic structure of a protein?
A polypeptide chain is a sequence of amino acids that forms the primary structure of a protein. This chain is held together by peptide bonds between adjacent amino acids.
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.
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 is a difference in the structure of proteins and polysaccharides?
Polysaccharides are essentially many carbon sugar "rings" linked together. They are carbohydrates, and our bodies break them down into monosaccharides (single "rings") to gain energy. To provide energy is their main function. In contrast, a peptide bond is formed between two amino acids via dehydration synthesis. Amino acids are the monomers for proteins within the body, who function in part to catalyze reactions and carry out other directions of DNA. Many peptide bonded amino acids = a polypeptide. The most basic difference would be that polypeptides are proteins, where as polysaccharides are carbohydrates.
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 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.
