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What level of protein structure characterized by coils and folds results from hydrogen bonding between carboxyl and amino groups of the polypeptide chain?
Wiki User
∙ 11y ago
I believe it is the secondary level. The secondary level is characterized by coils and folds (called pleats) as the bonds take place.
Wiki User
∙ 11y ago
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.
Wiki User
∙ 11y ago1) hydrogen bonding between polar side groups in the polypeptide chain;
2) cysteine disulfide bridges
Wiki User
∙ 11y agoA long chain of amine acids, bonded by pep-tide bond, twist and fold to form protein.
Wiki User
∙ 10y agoSecondary
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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.
Does carboxyl group do covalent bonds with another carboxyl group?
No. But hydrogen bond can be formed between two carboxyl groups.
Does a carboxyl group contain nitrogen?
No, a carboxyl group contains a carbon atom, an oxygen atom, and a hydrogen atom. It does not contain nitrogen.
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.
What is the difference between interchain and intrachain hydrogen bonds in the secondary structure of proteins?
Interchain hydrogen bonds form between different protein chains, such as in a multimeric protein complex. Intrachain hydrogen bonds form within the same protein chain, stabilizing the secondary structure, such as alpha helices or beta sheets. Both types of hydrogen bonds contribute to the overall stability and structure of proteins.
Which primarily responsible for the helical structure of a polypeptide chain?
Hydrogen bonding
The backbone of a polypeptide could be represented by?
The backbone of a polypeptide is formed by a repeating sequence of amino acids linked by peptide bonds. This linear chain has a specific orientation with an N-terminus and C-terminus. The backbone provides structural support and flexibility to the polypeptide, allowing it to fold into a specific 3D shape.
Betta pleated sheets are characterized by?
folds stabilized by hydrogen bonds between segments of the polypeptide backbone.
Hydrogen bonds between different parts of the polypeptide chain result in which level of protein structure?
Tertiary structure
Some regions of a polypeptide may coil or fold back on themselves?
secondary structure ,hydrogen bonds
Does carboxyl ionize?
Yes, carboxyl groups ionize in solution by releasing a proton from the carboxylic acid group. This results in the formation of carboxylate ions. The extent of ionization depends on the pH of the solution.
What are the forces which create the tertiary structure of a polypeptide?
Four of them are; hydrophobic and hydrophilic interactions, hydrogen bonding and disulphide bridging.
Does carboxyl group do covalent bonds with another carboxyl group?
No. But hydrogen bond can be formed between two carboxyl groups.
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.
Does a carboxyl group contain nitrogen?
No, a carboxyl group contains a carbon atom, an oxygen atom, and a hydrogen atom. It does not contain nitrogen.
What is the level of protein structure that describes all aspects of the three-dimensional folding of a polypeptide?
Primary: Simple string of amino acids called a polypeptide. Secondary: The varied hydrogen bonding of the side chains resulting in alpha helixes and beta sheets. Tertirary: The R group bondingd; hydophobic, hydrophilic, hydrogen bonding and disulfide bonding, which results in the globular, actual protein. Quarternary: The construction of multi protein subunits from tertiary structure. Such as hemeglobin.
What must be done to a polypeptide chain to make it a functioning protein?
A protein becomes functional only when it folds itself into a three dimensional form or tertiary structure. More information - All amino acids have the same basic structure - an amino group, a carboxyl group and a hydrogen atom but they differ due to the presence of the side chain. The sequence of amino acids in a protein determines it's primary structure
