Consider a alpha-helix "stretch" of a protein consisting of 20 amino acid residues compared to a...

Consider a alpha-helix "stretch" of a protein consisting of 20 amino acid residues compared to a Beta-strand "stretch" of a protein consisting of 20 amino acids(which of course is part of a Beta-sheet). What is the length of this alpha-helix and Beta-strand portion of the protein in angstroms?

Solutions

Expert Solution

Ans. # One turn (a repeating unit) of a-helix consists of 3.6 residues with a pitch of 5.4 A.

So,

Length of a-helix = (Pitch of helix) x Number of residues in helix

= (5.4 A / 3.6 residues) x 20 residues

= 30.0 A

# The repeating unit of antiparallel b-sheet consists of 3 residues with a length of 7.0A.

Length of b-sheet = (Length of repeating unit) x Number of residues in b-sheet

= (7.0 A / 3 residues) x 20 residues

= 46.67 A

# The repeating unit of parallel b-sheet consists of 3 residues with a length of 6.5A.

Length of b-sheet = (Length of repeating unit) x Number of residues in b-sheet

= (6.5 A / 3 residues) x 20 residues

= 4.33 A

queen_honey_blossom answered 1 year ago

Next > < Previous

Related Solutions

1). Where do the hydrophobic amino acid residues usually end up in a folded protein and...

1). Where do the hydrophobic amino acid residues usually end up in a folded protein and why? How does hydrogen bonding play a role in stabilizing the beta-sheet structure? Where do the R groups then end up in this structural pattern? 2). Why is the alpha-helix so commonly found? Describe the structural basis of this conformation. 3). How do amyloid-beta peptides aggregate and eventually cause Alzheimer's disease? Where do the amyloid-beta peptides come form (what protein are they from and...

How do hydrophobic and hydrophilic amino acid residues affect how a protein is folded? Include in...

How do hydrophobic and hydrophilic amino acid residues affect how a protein is folded? Include in your response these two examples of proteins: membrane protein and cytosolic protein.

Describe the properties of an amphipathic alpha helix and identify numbered amino acids in a dodecamer...

Describe the properties of an amphipathic alpha helix and identify numbered amino acids in a dodecamer polypeptide that contribute to the chemical properties of this secondary protein structure. Where are amphipathic alpha helices found in a globular cytosolic protein?

Indicate which of the amino acid residues in the following peptide sequence contains a group that...

Indicate which of the amino acid residues in the following peptide sequence contains a group that has a negative charge for its most likely charge state at pH 4. Met-Tyr-Ile-Trp-Gln-Val-Cys-Pro-Lys

What do you think your 93rd amino acid is for this protein? the amino acid sequence...

What do you think your 93rd amino acid is for this protein? the amino acid sequence of the protein coded for by the wild-type TYRP1 is just below.

What would be the expected orientation of an amphipathic alpha helix occurring in a globular protein...

What would be the expected orientation of an amphipathic alpha helix occurring in a globular protein in aqueous solution? Select one: a. Hydrophilic amino acids are complementary to hydrophobic amino acids, so the hydrophilic side of the alpha helix should be facing toward the hydrophobic core of the protein. b. A soluble protein will have mostly hydrophilic amino acids in its core, so the helix will be arranged to have the hydrophilic side facing toward the core of the protein....

Two amino acids are either not a standard alpha- amino acid or in the S configuration....

Two amino acids are either not a standard alpha- amino acid or in the S configuration. Which residues are they, and how are they different? Illustrate your reasoning with chemical structures

“Protein A” is phosphorylated at one amino acid by a kinase, “protein B”, and dephosphorylated by...

“Protein A” is phosphorylated at one amino acid by a kinase, “protein B”, and dephosphorylated by a phosphatase, “protein C”. You have purified all three of these proteins and want to determine the structural changes that occur when protein A is phosphorylated or dephosphorylated. Explain in detail how you would go about designing and conducting this investigation.

“Protein A” is phosphorylated at one amino acid by a kinase, “protein B”, and dephosphorylated by...

“Protein A” is phosphorylated at one amino acid by a kinase, “protein B”, and dephosphorylated by a phosphatase, “protein C” You want to determine the mechanisms of protein B and C. What experimental information would you need in order to propose a reasonable mechanism? Explain.

If hemoglobin has a mutation of the following amino acid residues: His 2, His 143, and...

If hemoglobin has a mutation of the following amino acid residues: His 2, His 143, and Lys 82 which have caused them to be changed to aspartic acid residues, how does this alter hemoglobin’s function? Specifically discuss how this could affect binding with the expected ligand at this site (name this ligand and describe if this interaction be stronger or weaker) and the overall effect to oxygen binding capacity and affinity these mutations have relative to the wild type hemoglobin...

Subjects