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The primary structure of a folded protein is?
The primary structure of a folded protein is the linear sequence of amino acids linked together by peptide bonds. This sequence is derived from the protein's genetic information and serves as the foundation for its three-dimensional shape and function.
When a polypeptide is folded it is called what?
When a polypeptide is folded into its three-dimensional structure, it is referred to as a protein. Proteins are made up of one or more polypeptide chains that have folded into a specific conformation to perform their biological functions.
what is a biomolecular structure?
Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.
What level of molecular organization is a beta-folded sheet?
A beta-folded sheet is a secondary structure of a protein, which is the next level of molecular organization above the primary structure. It is formed by hydrogen bonding between adjacent segments of a polypeptide chain, creating a flat and elongated sheet-like structure.
A protein folded into a globular shape in having only one polypeptide chain has what structure?
The protein would have a tertiary structure. This structure results from the unique folding of the single polypeptide chain into a 3D shape, giving the protein its functional conformation.
How does a DNA molecule determined the structure of a protein?
The DNA sequence will determine the amino acid sequence known as the protein's primary structure. As the protein is folded into the secondary, tertiary and quatranary structures, the amino acid molecules will determine the shape
What is the difference between a domain and a motif in the context of protein structure?
In the context of protein structure, a domain is a distinct and independently folded region of a protein that performs a specific function. A motif, on the other hand, is a smaller, recurring structural pattern within a protein that may not have a specific function on its own but contributes to the overall structure and function of the protein.
What term is used to describe the arrangement of different polypeptide chains in a protein?
The term used to describe the arrangement of different polypeptide chains in a protein is "quaternary structure." This structure refers to the spatial arrangement of multiple folded protein subunits held together by non-covalent interactions, forming a functional protein complex.
What is a denatured protein?
A denatured protein is a protein whose structure has been altered, leading to loss of its function. Denaturation can be caused by heat, pH changes, or exposure to chemicals, resulting in unfolding or disruption of the protein's folded structure.
What does a protein look like and how is its structure defined?
A protein is a complex molecule made up of chains of amino acids folded into a specific shape. Its structure is defined by the sequence of amino acids and how they interact with each other through various bonds and interactions. This unique structure determines the protein's function in the body.
What is the main structure of protein molecules?
Proteins are made up of long chains of amino acids that are folded into a specific 3D structure. This structure is crucial for the protein to function properly. The primary structure refers to the specific sequence of amino acids in the chain, while the secondary structure involves the folding of the chain into alpha helices and beta sheets. Tertiary structure refers to the overall 3D shape of the protein, while quaternary structure involves the arrangement of multiple protein subunits.
Largest contribution to the stability of a folded protein?
The largest contribution to the stability of a folded protein is typically due to hydrophobic interactions between nonpolar residues within the protein core. These interactions help bury hydrophobic groups away from the surrounding solvent, minimizing solvent exposure and increasing the overall stability of the folded structure. Additional contributions can come from hydrogen bonds, electrostatic interactions, and disulfide bonds.
