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A regular element of secondary structure in proteins, in which two or more extended strands of the polypeptide chain lie side by side (running either parallel or antiparallel), held together by a regular array of hydrogen bonds between backbone NH and C=O groups, to form a ridged planar surface. The amino-acid side chains alternately face to opposite sides of the sheet.

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Do amino acids contain alpha and beta pleated sheet in their secondary structure?

Yes, they do. Side group hydrogen bonding.


The alpha helix and beta pleated sheet represent which level of protein structure?

The alpha helix and beta pleated sheet represent the secondary structure of proteins. Both structures are formed by the interaction of amino acids within the polypeptide chain through hydrogen bonding.


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.


What level of molecular organization is a beta-folded sheet?

A beta-folded sheet is a secondary structure of a protein, which is the next level of molecular organization above the primary structure. It is formed by hydrogen bonding between adjacent segments of a polypeptide chain, creating a flat and elongated sheet-like structure.


What level of protein structure is associated the alpha helix and beta pleated sheet?

It depends on the primary sequence of amino acids as to which secondary structure is more stable. Both structures use hydrogen bonds to stabilize the structures, however in an alpha helix, these hydrogen bonds are with the peptide and in beta sheets the hydrogen bonds are between beta peptide strands. I really don't know which structure is more stable... -alpha helix seems to be a more common structure -and B sheets lose some H bonding during hair pin turns and during twists. -But an alpha helix has a dipole whereas an antiparalle beta sheet doesnt. -weighing it up i would assume an alpha helix to be more stable but that would be a guess from me.

Related Questions

Structure of keratin?

Alpha keratin has alpha helix structure and beta keratin has beta pleated sheet structure.


Do amino acids contain alpha and beta pleated sheet in their secondary structure?

Yes, they do. Side group hydrogen bonding.


A pleated sheet organization in a polypeptide chain is an example of which structure?

A pleated sheet organization in a polypeptide chain is an example of secondary protein structure, specifically beta sheet secondary structure. It involves hydrogen bonding between neighboring polypeptide strands running in opposite directions.


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.


The alpha helix and beta pleated sheet represent which level of protein structure?

The alpha helix and beta pleated sheet represent the secondary structure of proteins. Both structures are formed by the interaction of amino acids within the polypeptide chain through hydrogen bonding.


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 levels of protein folding would include shapes identified as helix and pleated sheet?

The secondary level of protein folding includes the formation of alpha helices and beta sheets, which are common in protein structures. These structures result from hydrogen bonding between amino acids in the protein chain, leading to the characteristic helical or sheet-like shapes.


Do the coils and folds of a protein's amino acid chain make up the protein's primary structure?

The coils of an alpha helix or the folds of a beta-pleated sheet are a characteristic of the secondary structure.


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.


Can paper shield beta particles?

Beta particles are not stopped by a paper sheet.


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.


What does Alpha helix and beta pleated sheets make up?

together they make a secondary protein structure