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protein secondary structures, which are common motifs found in protein folding. Alpha helices are formed by a right-handed coil of amino acids stabilized by hydrogen bonding, while beta-pleated sheets are formed by hydrogen bonding between adjacent strands of amino acids running in parallel or antiparallel orientation.
What else can I help you with?
Which type of interaction stabilizes the alpha helix and the beta pleated sheets of a protein?
Hydrogen bonding is the primary interaction that stabilizes the alpha helix and beta pleated sheets of a protein. In the case of alpha helices, hydrogen bonds form between the carbonyl oxygen of one amino acid residue and the amide hydrogen of another residue in the chain. In beta sheets, hydrogen bonds form between adjacent strands of the sheet.
Is it aminoaacids that are the secondary structure of alpha helix and beta pleated?
The secondary structures of alpha helix and beta pleated sheets are formed by hydrogen bonding between amino acids in a protein chain. In an alpha helix, the hydrogen bonding occurs between amino acids in the same chain, leading to a helical structure. In beta pleated sheets, hydrogen bonding occurs between amino acids in different segments of the protein chain, creating a sheet-like structure.
What absorbs alpha radiation?
Pretty much anything will. A couple of sheets of paper would do it. Alpha radiation is big and bulky compared to other types of radiation. So it can't penetrate objects very far.
Which type of radiation can pass easily through polythene sheets?
Alpha radiation cannot easily pass through polythene sheets, while beta and gamma radiation can pass through them. However, beta radiation may be partially absorbed depending on the energy level.
What is the difference between alpha percival and alpha percival cyclone?
Alpha Percival Cyclone Can spin
What does a protein's alpha helices and beta sheets fold together to create?
Alpha helices and beta sheets fold together to create the secondary structure of a protein, forming the protein's overall 3D shape. This structure helps determine the protein's function by influencing how it interacts with other molecules in the body.
What type of secondary structure does hemoglobin have?
Hemoglobin is a protein with a combination of secondary structures, predominantly consisting of alpha helices and beta sheets. These structural elements help maintain the shape and function of hemoglobin as a globular protein.
Does amylase contain both an alpha helix and a beta pleated sheets?
Yes, amylase contains both alpha helices and beta pleated sheets in its secondary structure. These structures are important for maintaining the enzyme's functional conformation and catalytic activity.
How many beta sheet hemoglobin have?
Hemoglobin does not contain beta sheets. It is a globular protein composed of four subunits - two alpha and two beta subunits in adults (hemoglobin A). Each subunit consists of alpha-helices, not beta sheets.
Where can one find more information about alpha helices?
One can find information about alpha helices in your local library.You could find about all other helices in that category and how they are used in life.
Do all proteins contain alpha helixes and beta pleated sheets?
Not all proteins contain alpha helices and beta pleated sheets. These structures are specific types of secondary protein structures typically found in many proteins, but some proteins may lack these features entirely. The presence of alpha helices and beta sheets depends on the protein's amino acid sequence and overall folding. Some proteins may adopt entirely different conformations or structures, such as random coils or unique motifs.
What type of structure does hemoglobin have?
Alpha helices
What elements of protein secondary structure are present in this structure?
The protein structure contains both alpha helices and beta sheets, which are the two main elements of protein secondary structure.
What structure of proteins is determined by the hydrogen bonds between amino acids that cause the protein to coil into helices or pleated sheets.?
The structure of proteins that is determined by hydrogen bonds between amino acids, causing the protein to coil into helices or form pleated sheets, is known as secondary structure. This level of organization arises from the interactions between the backbone atoms in the polypeptide chain, leading to common structural motifs such as alpha helices and beta sheets. These configurations are crucial for the overall stability and function of the protein.
Which type of interaction stabilizes the alpha helix and the beta pleated sheets of a protein?
Hydrogen bonding is the primary interaction that stabilizes the alpha helix and beta pleated sheets of a protein. In the case of alpha helices, hydrogen bonds form between the carbonyl oxygen of one amino acid residue and the amide hydrogen of another residue in the chain. In beta sheets, hydrogen bonds form between adjacent strands of the sheet.
Which of these proteins in mammals show only primary and secondary structures?
Collagen and keratin are examples of proteins in mammals that primarily exhibit only primary and secondary structures. Collagen is known for its triple helix structure, while keratin is a fibrous protein that forms alpha-helices and beta-sheets.
What can form a structure such as a helix or a sheet?
Proteins can form structures such as a helix or a sheet due to the specific arrangement of amino acids in their sequence. The hydrogen bonding between the amino acids in the polypeptide chain determines the secondary structure of the protein, leading to the formation of helices and sheets.
