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In a new protein structure you just solved by X-ray crystallography, you see a very long a-helix containing 36 amino acids. what is the length of this helix? (give both in angstroms and in nm)

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Beverley Smith
Beverley SmithLv2
28 Sep 2019

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Related questions

2. From studies of chemistry, we know that in a straight chainhydrocarbon, such as a fatty acid, each methylene group lengthensthe chain by about 0.13 nm. From studies of protein structure, weknow that one turn of an α-helix takes 3.6 amino acid residues andlengthens the axis of the helix by about 0.56 nm. Using thisinformation, answer the following questions: (Answer parts a-c toone decimal place in units of nm, e.g. 9.0 nm.)

a. (1 pt) Using this information, how thick is the non-polarcore of the bilayer containing the GLUT1 transporter (i.e. what isthe length of each helix)?

b. (1 pt) How many fatty acid methylene groups would be neededto span this distance? (Round to closest whole number.)

c. (1 pt) Since fatty acids in membrane lipids always have aneven number of carbons in their chains, what chain lengths might becommon in this membrane? (Write the number of carbons. More thanone number may be correct.)

d. (2 pts) Most membrane lipids have 16 or 18 carbons, how canthe length of these fatty acids be accommodated in themembrane?

1) Explain the difference between alpha helices, parallel beta sheets and antiparallel sheets in terms of shape and hydrogen bonding orientation.

2) You discover a new protein tetramer, and determine that each monomer consists of a single alpha helix that is 17 amino acids long. Sequence analysis of the protein indicates that the helix contains a mix of polar, charged and hydrophobic residues. You find that the hydrophobic residues are located at positions 1,2,5,6,9,10,13,14 and 17 of the helix. The protein is water soluble. In pictures or in words, describe the quaternary structure of this protein.

1) Which three amino acids are most the frequent targets of post-translational modification via phosphorylation?

A) cysteine, proline, serine

B) proline, serine, tyrosine

C) serine, threonine, tyrosine

D) arginine, aspartic acid, glutamic acid

2) In an alpha helix structure of a protein, the amino acid side groups are positioned...

A) in the hydrophobic interior of the helix (this is not the right answer, I put this answer choice already and it was wrong)

B) in the interior of the hydrophilic interior of the helix

C) outside of the helix

D) on both the outside and inside of the helix

E) None of the above. Amino acids in alpha helices do not have side groups.

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