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At which level of protein structure are interactions between the side chains of R groups and other groups the most important?
Wiki User
∙ 15y ago
The first level
Wiki User
∙ 11y ago
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Differentiate the four types of protein structure?
There are four types of protein structure. These include primary structure, secondary structure, tertiary structure, and quaternary structure. Primary structure is the amino acid sequence. Secondary structure is the shape of the molecule. Tertiary structure is the interaction between groups. Quaternary structure is the interactions between protein subunits.
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.
How does the shape of a protein change as it goes from primary to quaternary?
The primary structure of a protein is the unique sequence of amino acids. There are 20 possible amino acids, and the primary structure consists of a string of amino acids held together by peptide bonds. The secondary structure occurs when the amino acid chain becomes coiled or folded in alpha helix or beta pleated sheets. The protein develops its three-dimensional shape in the tertiary structure. Van der Waals interactions, disulfide bonds, hydrophobic interactions, and ionic bonding all impact the tertiary structure. Finally, the quaternary structure is made up of more than one polypeptide chain (a polypeptide chain is the string of amino acids described in the primary structure). Hope this helps!
Hydrogen bonds between different parts of the polypeptide chain result in which level of protein structure?
Tertiary structure
Explain what determines protein confirmation and why it is important?
Environment and bonding. The structure determines its function.
Differentiate the four types of protein structure?
There are four types of protein structure. These include primary structure, secondary structure, tertiary structure, and quaternary structure. Primary structure is the amino acid sequence. Secondary structure is the shape of the molecule. Tertiary structure is the interaction between groups. Quaternary structure is the interactions between protein subunits.
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.
The tertiary structure of a protein is the?
Is the many foldings and twists resulting from the interactions of the R group side chains; hydrophobic interactions, hydrogen bonding between polar groups, ionic bonding between charged groups, hydrophyllic interactions and covalent bonding between sulfur containing groups. All this contributes to the globular or other shape the mature protein will take.
Is protein's primary structure formed by hydrophobic interactions?
Ni, just peptide bonding. Hydrophobic interactions do not have significance to folding until tertiary structure folding.
What are the four stages of protein structures?
The four levels of protein structure are differentiated from each other by the complexity of their polypeptide chain. Proteins are constructed from 20 amino acids. The levels are the hydrogen atom, a Carboxyl group, an amino group and a variable or "R" group. They have a primary structure, the order in which the amino acids are linked to form a protein. Secondary structure , coiling and folding of the polypeptide chain. Tertiary structure, is a 3-D structure of a protein chain. Quaternary is the structure of a protein macro molecule formed by interactions between several polypeptide chains..
How does protein denatured?
It breaks the hydrogen bonds and hydrophobic interactions between different parts of the protein molecule. Proteins are composed of amino acid subunits linked together by peptide bonds—this is called a polypeptide and is also known as the primary structure of a protein. The primary structure interacts with itself (also known as folding) forming hydrogen bonds and hydrophobic interactions with different parts of the same molecule. Heat disrupts the hydrogen bonds and hydrophobic interactions leaving the protein to unfold when it is heated. Since heat is not strong enough to break the peptide bonds between the amino acid subunits, the primary structure remains intact. Once the protein is cooled again, the hydrogen bonds and hydrophobic interactions can reform since they are based on the makeup of the primary structure and it hasn't changed. :) Hope this helps.
How does heat denatured protein?
It breaks the hydrogen bonds and hydrophobic interactions between different parts of the protein molecule. Proteins are composed of amino acid subunits linked together by peptide bonds—this is called a polypeptide and is also known as the primary structure of a protein. The primary structure interacts with itself (also known as folding) forming hydrogen bonds and hydrophobic interactions with different parts of the same molecule. Heat disrupts the hydrogen bonds and hydrophobic interactions leaving the protein to unfold when it is heated. Since heat is not strong enough to break the peptide bonds between the amino acid subunits, the primary structure remains intact. Once the protein is cooled again, the hydrogen bonds and hydrophobic interactions can reform since they are based on the makeup of the primary structure and it hasn't changed. :) Hope this helps.
Why small molecule - protein interactions are generally domninated by hydrophobic interactions?
An example of the protein-protein interactions is the antigen-antibody interactions. Because of the complexity of the protein molecules, the hydrophobic interactions are more dominant.
Why is the sequence of DNA important?
It determines protein structure.
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.
How does high temperature affect tertiary structure of a protein?
High temperature denatures most proteins. This means that the 3D structure (tertiary and quaternary structure) changes in a way that the molecule loses its biological function. Denaturation by heat is irreversible.
Why is a protein denatured?
depending upon the normal environment of the given protein, the secondary, tertiary, and the quaternary structure of the protein depend upon interactions between the amino acids of the protein itself within the structure of the protein, and interactions with the environment surrounding the proteinas an example:a protein that normally exists in an aqueous (mostly water) environment will have a structure in which the non-polar amino acids in large part will be confined to the interior of the structure where they will not interact with the aqueous exterior environment, as well as polar or charged amino acids on the exterior interacting with water, cytosolic fluid, or other polar substances.this occurs because non-polar amino acids do not interact favorably with polar solvents-just as non-polar cooking oil separates from highly polar water- and are at the lowest possible energy state when they are not interacting with polar substances. this normal interaction of proteins makes their usual conformation the most thermodynamically stable which is why they exist in solution in said conformation.Short answer: see belowif the environment is changed from polar to non-polar then the intermolecular interactions between the solvent and the amino acids of the protein will change, which would cause change of conformation of the protein structure, and thus possibly cause denaturation because as we all know from BIO 101: structure determines function.
