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What levels of protein structure would be affected if all hydrogen bonding interactions were prevented?
Wiki User
∙ 10y ago
I don't get the question, but it won't work if its hydrogen bonds are broken.
Wiki User
∙ 12y ago
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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.
What determines which nitrogen bases form pairs in DNA?
Basically, their structure and geometry. Some of them "fit" together nicely with favorable hydrogen bonding interactions, and others don't.
What are three types of chemical interactions found in proteins?
Hydrogen bondsDisulfide bonds/bridgesDipole-dipole interactions
Give you the structure and composition of isotopes of hydrogen and carbon?
what is the structure of isotopes of hydrogen and carbon
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.
What structural level of a protein most affected by a disruption in hydrogen bonding?
The structural level of a protein is most affected by disruption would be the secondary structure. It is within the secondary structure where the folding and coiling of the protein is stabilized by hydrogen bonds.
What are the forces which create the tertiary structure of a polypeptide?
Four of them are; hydrophobic and hydrophilic interactions, hydrogen bonding and disulphide bridging.
What bonds are present in each of the four different levels of protein structure?
Primary- Covalent bonds Secondary- Hydrogen bonds Tertiary- Hydrophobic interactions - Disulphide bonds/bridges - Hydrogen bonding Quaternary- (Same as Tertiary)
Differentiate between secondary and tertiary structure by describing the parts of the polypeptide chain that participates in the bonds that hold together each level of structure?
Secondary tertiary is the R groups interactions that are ionic. The polypeptide chain also has disulfide bond, and hydrophobic interactions.
Is hydrogen affected by the sun?
no hydrogen is not affected by the sun because hydrogen can be combined with helium it creates a fuel source but it is not affected by hydrogen by it self so no hydrogen is not affected by the sun
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.
Does Hydrogen Bromide exhibit dipole-dipole interactions?
Yes. Hydrogen bromide shows dipole-dipole interactions.
What five forces are responsible for stabilisation of protein tertiary structure?
There's a few but some of them are:- hydrogen bonding hydrophobic interactions electrostatic interactions van der waals forces disulphide forces salt bridges.
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.
What determines which nitrogen bases form pairs in DNA?
Basically, their structure and geometry. Some of them "fit" together nicely with favorable hydrogen bonding interactions, and others don't.
Which is stronger dipole-dipole interactions or hydrogen bonds?
hydrogen bonding is stronger.
Why is the primary structure of a protein unaffected by heating?
Primary structure is a sequence of amino acid joined covalently unlike hydrogen/ ionic bond, which is easily affected by heat, in 2' 3' 4' structures.
