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locations of key amino acids allows for association through hydrogen bonding

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13y ago

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Are parallel or antiparallel beta sheets stronger in protein structures?

Antiparallel beta sheets are generally stronger in protein structures compared to parallel beta sheets.


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 does Alpha helix and beta pleated sheets make up?

together they make a secondary protein structure


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.


Why are parallel beta sheets less stable than anti-parallel beta sheets in a folded protein molecule?

Parallel beta sheets are less stable than anti-parallel beta sheets because of the weaker hydrogen bonding interactions between strands in parallel sheets. The alignment of hydrogen bond donors and acceptors in parallel beta sheets reduces the strength of hydrogen bonds, leading to lower stability. In anti-parallel beta sheets, the hydrogen bonds are more linear and therefore stronger, enhancing the overall stability of the structure.


What is bridging sheet in HIV?

The unique Protein Fold of HIV, maily consisting of 2 beta-sheets.


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.


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 is the process by which heat or acidity disrupts the normal shape of a protein?

Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a random shape


What is a silk protein?

Protein found in silk,a strong,soft,lustrous fibre made of fibroin, a structural protein consisting almost entirely of stacked antiparellel beta plated sheets.


What is it called when protein unfolds?

The process of a protein unfolding is called denaturation. During denaturation normal alpha-helix and beta sheets are disrupted causing the protein to uncoil and become misshaped


What is the process by which heat or acidity disrupts the normal shape of a protein chain?

Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a random shape