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The foldings of the tertiary structure are generally monitored by proteins called "chaperonins". These protein complexes have two rings that are stacked on top of each other like a cylinder. The complex has enough room to contain the polypeptide for folding into its 3-d shape.

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Which level of protein structure may be stabilized by covalent bonds?

Primary, tertiary and quaternary levels of protein structure.


What occurs in the tertiary but not primary structure of protein?

In protein structure, tertiary structure refers to the overall three-dimensional folding of a polypeptide chain, which is stabilized by various interactions such as hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. This level of structure is crucial for the protein's functionality and is not present in primary structure, which is merely the linear sequence of amino acids. While primary structure defines the sequence, tertiary structure determines how that sequence folds into a functional shape.


What is tertiary protein structure in DNA?

Tertiary protein structure refers to the three-dimensional arrangement of a protein's polypeptide chain, which is stabilized by various interactions, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. However, DNA itself does not have a tertiary protein structure, as it is a nucleic acid composed of nucleotides rather than amino acids. Instead, DNA can interact with proteins that have tertiary structures, such as histones and transcription factors, which help in the organization and regulation of genetic material.


What aspect of protein structure are stabilized or assisted by hydrogen bonds?

secondary, tertiary, and quaternary structures, but not primary structure


Why do all molecules of RNAasa have the same tertiary structure?

All molecules of ribonuclease A (RNase A) have the same tertiary structure because they are highly structured proteins with a specific fold determined by their amino acid sequence. This common structure includes characteristic alpha helices and beta sheets that are stabilized by hydrogen bonding and disulfide bonds, ensuring that the protein adopts the same shape in all instances.


What are 4 levels of protein?

Primary_structure: the Peptide_sequence.Secondary_structure: regularly repeating local structures stabilized by Hydrogen_bond. The most common examples are the Alpha_helix, Beta_sheetand Turn_(biochemistry). Because secondary structures are local, many regions of different secondary structure can be present in the same protein molecule.Tertiary_structure: the overall shape of a single protein molecule; the spatial relationship of the secondary structures to one another. Tertiary structure is generally stabilized by nonlocal interactions, most commonly the formation of a Hydrophobic_core, but also through Salt_bridge_(protein), hydrogen bonds, Disulfide_bond, and even Post-translational_modification. The term "tertiary structure" is often used as synonymous with the term fold. The Tertiary structure is what controls the basic function of the protein.Quaternary_structure: the structure formed by several protein molecules (polypeptide chains), usually called Protein_subunitin this context, which function as a single Protein_complex.


What are the 4 levels of proteins?

Primary_structure: the Peptide_sequence.Secondary_structure: regularly repeating local structures stabilized by Hydrogen_bond. The most common examples are the Alpha_helix, Beta_sheetand Turn_(biochemistry). Because secondary structures are local, many regions of different secondary structure can be present in the same protein molecule.Tertiary_structure: the overall shape of a single protein molecule; the spatial relationship of the secondary structures to one another. Tertiary structure is generally stabilized by nonlocal interactions, most commonly the formation of a Hydrophobic_core, but also through Salt_bridge_(protein), hydrogen bonds, Disulfide_bond, and even Post-translational_modification. The term "tertiary structure" is often used as synonymous with the term fold. The Tertiary structure is what controls the basic function of the protein.Quaternary_structure: the structure formed by several protein molecules (polypeptide chains), usually called Protein_subunitin this context, which function as a single Protein_complex.


What is it called when a protein folds back onto itself?

a. tertiary structure b. primary structure c. secondary structure d. tertiary structure pick your best answer


Is insulin a tertiary protein structure?

The active form of insulin, in the body, is a tertiary protein structure. However, when stored in the body, several insulin molecules are bound together in a hexamer (a six-protein quaternary structure).


What level of protein structure is stabilized by covalent?

Covalent bonds primarily stabilize the tertiary structure of proteins. This level of structure involves the overall three-dimensional arrangement of a polypeptide chain, including interactions between side chains, such as disulfide bridges formed between cysteine residues. These covalent interactions help maintain the protein's shape, which is crucial for its function.


What is 'tertiary'?

Tertiary means the third in order ,hierarchy or level in sequence in structure , event or activity.


What is the teritary structure of a protein?

The tertiary structure of a protein is just how a polypeptide folds up into a "glob" or a "pretzel-like" shape. Primary structure determines secondary and tertiary structure of a protein. Usually a tertiary protein is held together Disulfide bonds like those found in a Cysteine residue.