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What does a protein's alpha helices and beta sheets fold together to create?
Wiki User
∙ 10y ago
The question should be "what do alpha helices and beta sheets create?" They form the tertiary structure of proteins.
Wiki User
∙ 10y ago
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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.
What is the difference between interchain and intrachain hydrogen bonds in the secondary structure of proteins?
Interchain hydrogen bonds form between different protein chains, such as in a multimeric protein complex. Intrachain hydrogen bonds form within the same protein chain, stabilizing the secondary structure, such as alpha helices or beta sheets. Both types of hydrogen bonds contribute to the overall stability and structure of proteins.
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.
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 structure refers to local folding patterns involving hydrogen bonding between the peptide backbone, forming alpha helices or beta sheets. Tertiary structure involves the overall 3D folding of the entire polypeptide chain, with interactions between side chains such as hydrophobic interactions, hydrogen bonding, disulfide bridges, and electrostatic interactions playing a major role in maintaining the structure.
Can silver be hammered into sheets?
Yes, silver can be hammered into sheets, a process known as silver sheet metalwork. The metal is heated to make it more malleable, then hammered using a technique known as planishing to create thin, flat sheets.
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 structure refers to local folding patterns involving hydrogen bonding between the peptide backbone, forming alpha helices or beta sheets. Tertiary structure involves the overall 3D folding of the entire polypeptide chain, with interactions between side chains such as hydrophobic interactions, hydrogen bonding, disulfide bridges, and electrostatic interactions playing a major role in maintaining the structure.
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.
How enzymes are globular?
Besides fibrous proteins, that have only one type of secondary structure, globular proteins, including enzymes, transport and structural proteins, some peptide hormones, and immunoglobulins, are folded structures much more compact than alpha (helices) or beta (sheets) conformations.Moreover, globular proteins, with random or repetitive conformations, have roughly spherical shapes. Globular proteins usually exhibit little or no change untill a point is reached at which there is a sudden drastic change and, invariably, a loss of biological function (e.g., structural proteins) or their enzymatic activity (for enzymes), a phenomenon known as denaturation.Finally, to understand the terciary structure of globular proteins there are two powerful techniques to do it: X-ray or neutron diffraction analysis of single crystals, and NMR analysis (Nuclear Magnetic Resonance) of small proteins in solution.
