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What are the forces which create the tertiary structure of a polypeptide?
Wiki User
∙ 14y ago
Four of them are; hydrophobic and hydrophilic interactions, hydrogen bonding and disulphide bridging.
Wiki User
∙ 14y ago
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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!
If a protein contains three polypeptide chains that are held together by bonding forces what kind of structure does the protein have?
The protein has a quaternary structure.In addition, each polypeptide chain has a primary, secondary, and tertiary structure.The primary structure is the sequence of amino acids in a chain.The secondary structure is the next higher level of arrangement of a chain in space, for example coiling into a alpha-helix, shaping into a beta-pleated sheet, or forming into a turn or loop.Tertiary structure is a yet higher-level folding of the chain into its final three-dimensional shape.Some proteins have only one chain, but if there are two or more, the combination of these chains to form the functional protein is the quaternary structure.
How do you predict the 3-D structure of a protein with respect to bio-informatics?
There are three main protein structures. Primary, secondary, and tertiary.Primary Structure:- This structure consists of a linear, unbranched polypeptide strand. This structure is established by covalent bondingSecondary Structure:- There are two different types of secondary structures of proteins; α-helix and β-pleated. This type of protein structure is maintained by hydrogen bonding. An example of a α-helix is DNA.Tertiary Structure:- This is structure is maintained by Hydrogen bonding, disulfide linkages and van der Waals forces. It usually consists of two or more polypeptide chains. An example is the K+/Na+ pumps found on the surface of the plasma membrane.And, for proteins constituted by more than one polypeptidic chain, there's also a Quaternary Structure, which results from the association among the chains. As examples, insulin and hemoglobin are proteins with quaternary structure.
Does amino acid contain protein?
Proteins contain amino acids. Amino acids are the monomers and are polymerised through condensation to form polypeptide chains. The polypeptide chains are then folded through various forces such as hydrogen bonding, ionic interactions etc. to form proteins.
What is the tertiary structure for a protein?
'The Quaternary structure of a protein is the 4th level of folding for a protein. An example of this would be a red blood cell, which is a quaternary structure, it is made up of alpha helicies and also beta pleated in the tertiary structure. The Quaternary structure of a protein contains 4 tertiary structures in it.
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!
If a protein contains three polypeptide chains that are held together by bonding forces what kind of structure does the protein have?
The protein has a quaternary structure.In addition, each polypeptide chain has a primary, secondary, and tertiary structure.The primary structure is the sequence of amino acids in a chain.The secondary structure is the next higher level of arrangement of a chain in space, for example coiling into a alpha-helix, shaping into a beta-pleated sheet, or forming into a turn or loop.Tertiary structure is a yet higher-level folding of the chain into its final three-dimensional shape.Some proteins have only one chain, but if there are two or more, the combination of these chains to form the functional protein is the quaternary structure.
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.
Which type of structure is most likely to be damaged when its parts act as levers and create very strong forces?
mass
What bonds do Tertiary and quaternary structure of proteins involve?
Several, and they are mostly the same as tertiary structure. Hydrogen bonding, London dispersion/Van der Waal's forces, dipole moments, disulfide bonds, and occasionally (such as in hemoglobin), ionic bonding.
Why is the intermolecular force of C2h6 London forces?
When you draw the molecular structure, the structure is in fact symmetrical. When the structure is symmetrical it is non-polar therefore the forces are said to be 'london forces'/ dispersion forces.
What is a redundant force?
redundant forces are the extra forces in a structure whose removal from a structure makes it statically determinate.for ex:in a structure of indeterminancy =2 ,2 forces can be removed
How do you predict the 3-D structure of a protein with respect to bio-informatics?
There are three main protein structures. Primary, secondary, and tertiary.Primary Structure:- This structure consists of a linear, unbranched polypeptide strand. This structure is established by covalent bondingSecondary Structure:- There are two different types of secondary structures of proteins; α-helix and β-pleated. This type of protein structure is maintained by hydrogen bonding. An example of a α-helix is DNA.Tertiary Structure:- This is structure is maintained by Hydrogen bonding, disulfide linkages and van der Waals forces. It usually consists of two or more polypeptide chains. An example is the K+/Na+ pumps found on the surface of the plasma membrane.And, for proteins constituted by more than one polypeptidic chain, there's also a Quaternary Structure, which results from the association among the chains. As examples, insulin and hemoglobin are proteins with quaternary structure.
What types of forces create landforms?
divergent, convergent, and transform are the types of forces that create landforms
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)
