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The question should be "what do alpha helices and beta sheets create?" They form the tertiary structure of proteins.

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Q: What does a protein's alpha helices and beta sheets fold together to create?
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What are the two most common secondary structures in a protein?

The two types of tertiary protein structures: globular and fibrous proteins. Globular proteins act as enzymes that catalyze chemical reactions in organisms. Fibrous proteins like collagen play structural role.


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.


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 are amino acids joined together to form a protein?

This is a strange question, considering that there are only 4 nucleotides that make up DNA! However, protein structure and function are determined by the primary structure (ie. the number and kinds of amino acids), but it's the variety of ways that these 20 amino acids can interact with each other that allows them to make such a large variety of proteins. Think about disulfide bond formations, b-sheets, a-helices, proteins forming dimers, trimers, etc. All these variations lead to the vast differences in proteins that are present in organisms. Or... Your amino acids are joined together through peptide bonds This chain of amino acids then folds into a secondary structure, and then folds some more until the protein is in its tertiary structure. The protein eventually folds into its native, biologically functional state


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.

Related questions

Can carbohydrates contain pleated sheets and helices?

No , these are present in proteins .


Do all proteins have quandary structure?

No. Proteins start out as a Primary structure, which is just the linear form and sequence of amino acids. The proteins then start forming alpha helices and/or Beta sheets depending on the properties of the amino acids. This is their Secondary structure The proteins then fold completely into tertiary structure. Here, we have a lot of hydrogen bonding and hydrophobic interactions within the protein between the helices and beta sheets. Many proteins are fully functional in their tertiary structure and don't have any reason for forming into a quaternary structure. In the quaternary structure, we usually see an interaction between 2 or more polypeptides or proteins. An example would be 2 proteins in their tertiary structure binding together to become a functional dimer. If 3 proteins were interacting it would form a trimer. Several proteins are functional only in a quaternary structure while several more proteins are just fine in their tertiary structure and therefore do not have a quaternary structure.


Name three typical shapes of protein molecules?

right handed alpha helices, left handed alfa helices, and beta sheets


What can form a structure such as a helix or a sheet?

A polypeptide chain, which is the primary structure of a protein, can fold into secondary structures such as an alpha-helix or a beta-sheet.


What are the two most common secondary structures in a protein?

The two types of tertiary protein structures: globular and fibrous proteins. Globular proteins act as enzymes that catalyze chemical reactions in organisms. Fibrous proteins like collagen play structural role.


What are the names and description of the four structures of proteins?

If meaning the four structural levels in proteins, then these are:* Primary structure, which is the sequence of amino acids in the peptide chain that constitutes the protein. * Secondary structure, is the location of formations called alpha-helices, beta-sheets and coiled coils (undefined, flexible structure), that forms with the help of hydrogen bonds between amino acids. * Tertiary structure: This is the over-all fold/structure of one peptide chain/protein, which can consist of many so called "domains" of typical structures of alpha-helices and beta-sheets. * Quaternary structure: Because some proteins are formed from many smaller subproteins (that is, by many peptide chains), quaternary structure describe how these subunits are assembled together.


How is the active site of enzyme formed?

Enzymes are proteins and as such, they undergo complex folding of the amino acid chain. They form globules, helices and sheets, among other structures. The pockets formed by such structures containing a functional group responsible for the reaction forms an active site.


Why is secondary called secondary?

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.


Why is it possible for cells to make thousands of different kinds of proteins with only a limited amount of amino acids?

You have four nucleic acids in DNA; Adenine, Guanine, Thymine, Cytosine. DNA is transcribed into mRNA, in which Thymine is basically replaced by Uracil. This mRNA goes outside of the nucleus and into the cytoplasm where protein translation occurs. For every three bases (for example, AGC, GTC, etc.) an amino acid is coded for.Now, there are 20 amino acids. They all fit into four categories - basic, acidic, non-polar, and polar, each group with different properties. If you have 20 amino acids, think of how many ways you can combine them to create different proteins, and how diverse proteins can be.A protein is not composed of a set number of amino acids. You start off with a primary structure, which is basically just a chain of amino acids, and then you get to the secondary structure, which are amino acid linked in either an alpha-helix or beta-pleated sheets. These alpha-helices or beta-pleated sheets can form together to make a tertiary structure. Tertiary structures are proteins in themselves.But these tertiary structures can interact together to form ANOTHER level of structure - quaternary structures! These are also proteins. An example would be hemoglobin, found in your bloodstream.So because the building blocks for proteins are 20 amino acids, there are a lot of possibilities for what you can make with them!


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.


What structure describes the alpha-helices and beta-sheets that are formed by hydrogen bonding vetween backbone atoms located near each other in the polypeptide chain?

This bonding is done in the secondary structure of the protein.


What are helix proteins?

There are no known proteins such as helix proteins. Alpha helix is a secondary structure element found in proteins that formed by amino acids which can form helix. Other secondary structures are beta sheets and random coils.