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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.
Proteins can be shaped as an alpha helix a beta pleated sheet or a glob?
Proteins can adopt various structural forms, including alpha helices, beta pleated sheets, and globular shapes, which are determined by their amino acid sequences and interactions. Alpha helices are coiled structures stabilized by hydrogen bonds, while beta pleated sheets consist of adjacent strands linked through hydrogen bonds, creating a sheet-like formation. Globular proteins, on the other hand, are more compact and spherical, often functioning as enzymes or hormones. These diverse shapes are crucial for the protein's specific functions in biological processes.
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.
Does polypeptide forms a pleated sheet or a helix as its tertiary structure?
Polypeptides can form both pleated sheets and helices, but these structures are typically associated with secondary rather than tertiary structure. In secondary structure, alpha helices and beta pleated sheets arise from hydrogen bonding between the backbone atoms of the polypeptide chain. Tertiary structure refers to the overall 3D shape of a polypeptide, which is determined by various interactions among side chains, including hydrophobic interactions, ionic bonds, and disulfide bridges.
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.
Proteins can be shaped as an alpha helix a beta pleated sheet or a glob?
Proteins can adopt various structural forms, including alpha helices, beta pleated sheets, and globular shapes, which are determined by their amino acid sequences and interactions. Alpha helices are coiled structures stabilized by hydrogen bonds, while beta pleated sheets consist of adjacent strands linked through hydrogen bonds, creating a sheet-like formation. Globular proteins, on the other hand, are more compact and spherical, often functioning as enzymes or hormones. These diverse shapes are crucial for the protein's specific functions in biological processes.
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.
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.
Can paper shield beta particles?
Beta particles are not stopped by a paper sheet.
