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What level of protein structure is represented by the coiling of the protein chain backbone into an alpha helix?
The coiling of the protein chain backbone into an alpha helix represents the secondary structure of a protein. This structure is stabilized by hydrogen bonds between the amino acid residues in the protein chain, forming a corkscrew-like structure.
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.
Why protein is called primary structure?
Proteins *have* primary, secondary, tertiary, and quarternary structures. The primary structure is simply the chain of amino acids without any other structure. Secondary structure results from folding of the chain to form rudimentary structures such as alpha helices, beta sheets and turns. Tertiary structure results from the further folding of the protein with secondary structures into different 3D shapes by interactions between different parts of the secondary structure. Quarternary structure results from different proteins with tertiary structures coming together to form a protein complex.
Pleating or coiling is what protein sturcture?
Coiling is a common protein structure. It refers to the coiling of the polypeptide chain into an alpha-helix or a beta-sheet. Pleating is not a standard term but may refer to the folding of the protein chain into a more compact structure.
What characteristics of a protein remain after it is denatured?
When a protein is denatured, its molecular shape is altered. This alteration may or may not be reversible.What remains is the primary structure of the chain(s) of the protein, in other words the sequence of the amino acids.The tertiary structure referers to the overall three dimensional shape will be lost
What are the differences between the alpha chain and beta chain in terms of structure and function within a protein complex?
The alpha chain and beta chain in a protein complex differ in their structure and function. The alpha chain typically forms the core of the protein complex, providing stability and structural support. In contrast, the beta chain often plays a role in binding other molecules or ions, contributing to the overall function of the complex. These differences in structure and function allow the alpha and beta chains to work together to perform specific tasks within the protein complex.
What is the significance of the beta-branched side chain amino acid in protein structure and function?
The beta-branched side chain amino acid plays a significant role in protein structure and function by influencing the folding and stability of the protein. It can affect the interactions between different parts of the protein and its overall shape, which in turn can impact its function in biological processes.
What is the relationship between the N to C terminus in protein structure?
The relationship between the N-terminus and C-terminus in protein structure is that they are the two ends of a protein chain. The N-terminus is the starting point of the chain, while the C-terminus is the ending point. These termini play a crucial role in determining the overall structure and function of the protein.
What level of protein structure is represented by the coiling of the protein chain backbone into an alpha helix?
The coiling of the protein chain backbone into an alpha helix represents the secondary structure of a protein. This structure is stabilized by hydrogen bonds between the amino acid residues in the protein chain, forming a corkscrew-like structure.
How does trypsin digest protein?
Trypsin digests protein(polypeptide) by cleaving the peptide chain at specific sites. Trypsin cleaves the peptide chain after Lysine(K) or Arginine(R) residues (amino acids) except when followed by a Proline(P) residue. Generally, the tryptic digestion leaves behind the protein as peptide chains having none or one Lysine or Arginine residue. This property of trypsin is widely used to study the protein primary structure and identification of proteins by analysing the resultant peptides using mass sepectrometry (MS).
What is the difference between the N-terminus and C-terminus in a protein structure?
The N-terminus is the starting point of a protein chain, while the C-terminus is the end point. They are important for determining the overall structure and function of the protein.
What is the level of protein structure is the amino acid sequence of the protein?
The primary structure of a protein refers to the linear sequence of amino acids in the polypeptide chain. It is the simplest level of protein structure that ultimately determines the overall shape, function, and properties of the protein.
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.
The alpha helix and pleated sheet are examples of?
secondary protein structures formed by hydrogen bonds between the amino acids in a protein chain. They play a crucial role in determining the overall structure and function of proteins.
What purpose does the chain on the protein serve?
The chain structure of a protein determines its function. The sequence of amino acids in the protein chain ultimately determines how the protein will fold into its specific three-dimensional shape, which is critical for its functional properties. Additionally, the chain allows the protein to interact with other molecules in the body and carry out its specific biological roles.
What is a tertiary protein structure exemplified by?
A tertiary protein structure is the three-dimensional arrangement of a polypeptide chain. An example of a tertiary protein structure is the globular shape of enzymes like catalase or lysozyme. This structure is crucial for the protein's function as it determines the active sites and binding sites.
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.
