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How does high temperature affect tertiary structure of a protein?
Wiki User
∙ 6y ago
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.
Wiki User
∙ 14y ago
Wiki User
∙ 13y agoInput of energy (by increase in temperature) increases the kinetic energy of the atoms in the protein. As they vibrate more, the interactions between the atoms involved in secondary structure become disrupted and this causes the structure to denature.
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How does low pH affect secondary and tertiary protein structures?
A pH that is too acidic or basic for the protein will denature it - the bonds that connect the amino acids to each other for "folding" will break and the tertiary structure is no longer the correct structure for that protein.
How does the sequence of DNA affect the function of a protein?
The sequence of nucleotides in DNA molecule is equivalent and is closely related to an amino acid sequence in the protein molecule. If for any reason the sequence of DNA nucleotides changes it will be reflected in amino acid sequence in the protein. Moreover, the correct sequence of amino acid in the protein will form the correct three-dimensional structure, or tertiary structure, that will confer the biological activity to protein. If a wrong amino acid is translated from a mutated gene in the DNA could change the spatial structure of the protein and therefore modify or erase its biological function.
Chemical denaturation of protein?
Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains the same after a denaturation process. Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a random shape.Denaturation occurs because the bonding interactions responsible for the secondary structure (hydrogen bonds to amides) and tertiary structure are disrupted. In tertiary structure there are four types of bonding interactions between "side chains" including: hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic interactions. which may be disrupted. Therefore, a variety of reagents and conditions can cause denaturation. The most common observation in the denaturation process is the precipitation or coagulation of the protein.
Does amino acids affect protein functions?
The sequence of amino acids affects protein function. The three-dimensional structure of a protein determines its function. The three-dimensional structure of a protein is determined by the sequence of its amino acids.
What genetic disorder results in protein abnormalities?
All genetic disorders affect the structure of proteins.
How might placing a peptide into a non-polar solution affect the tertiary structure of the peptide?
Placing a peptide into a non polar solution can affect the tertiary structure. It can affect it by identify the relatively facile rotations.
How does low pH affect secondary and tertiary protein structures?
A pH that is too acidic or basic for the protein will denature it - the bonds that connect the amino acids to each other for "folding" will break and the tertiary structure is no longer the correct structure for that protein.
Why does the order of amino acid acids affect the structure of a protein?
The order of amino acids can affect the protein's shape.
How does the sequence of DNA affect the function of a protein?
The sequence of nucleotides in DNA molecule is equivalent and is closely related to an amino acid sequence in the protein molecule. If for any reason the sequence of DNA nucleotides changes it will be reflected in amino acid sequence in the protein. Moreover, the correct sequence of amino acid in the protein will form the correct three-dimensional structure, or tertiary structure, that will confer the biological activity to protein. If a wrong amino acid is translated from a mutated gene in the DNA could change the spatial structure of the protein and therefore modify or erase its biological function.
Chemical denaturation of protein?
Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains the same after a denaturation process. Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a random shape.Denaturation occurs because the bonding interactions responsible for the secondary structure (hydrogen bonds to amides) and tertiary structure are disrupted. In tertiary structure there are four types of bonding interactions between "side chains" including: hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic interactions. which may be disrupted. Therefore, a variety of reagents and conditions can cause denaturation. The most common observation in the denaturation process is the precipitation or coagulation of the protein.
Does amino acids affect protein functions?
The sequence of amino acids affects protein function. The three-dimensional structure of a protein determines its function. The three-dimensional structure of a protein is determined by the sequence of its amino acids.
How can the amino acid sequence determine protein shape and function?
Amino acids have different properties according to their R group. They can be negative, positive, aromatic, etc. - which will affect where that amino acid will be found, and what functions it will perform. For example, Glutamate and Aspartate are negative amino acids, and so are most likely to be found on the surface of proteins. Whereas Leucine and Methionine are hydrophobic, so they will be found in the interior of the protein. The sequence of amino acids causes the protein to fold in a certain way to find the most energetically and functionally favourable shape.
What genetic disorder results in protein abnormalities?
All genetic disorders affect the structure of proteins.
Changing one amino acid with a protein could change what about the protein?
It will depend on how different the amino acid is to the one it replaced. If the structure and/or charge is quite different, a change of one amino acid can change the entire 3D structure of the protein. This will affect the proteins function.
Why does the the order of amino acid affect the structure of a protein?
The order of amino acids can affect the protein's shape.
How can biomagnification affect tertiary levels?
by killing organisms
How the conditions under which rock form affect the physical stability of rocks?
The conditions that affect physical stability are heat, temperature, compression, pressure, and the molecular structure.
