Alpha helices are a type of secondary structure in proteins. What is the length of a 23.0 kDa single-stranded a-helical protein segment? Assume a mean residue mass of 110 Da. length: 209 Incorrect
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- SYNZIPS are a-helices that can be used in synthetic biology to create coiled-coil interactions between two different proteins. SYNZIP1 is around 47 amino acids in length. If each turn in an a-helix is 3.6 residues in length and each turn is 5.4 Å in length, how long is SYNZIP1? Keep in mind that 1 Å = 10 nm. Present your answer in nm.Given that an α helix has 3.6 residues per turn and the rise along the α helix axis is 5.4 Å, approximately how many amino acids would you find in a single contiguous α helix that is 210 Å long?Estimate the length, in nm, of the four identical beta-strands drawn in blue in panel (B) of the image below, if they consists of only the amino residues of the two alpha-helices highlighted in purple in panel (A) of the image below. Assume that the amino acid residues of the two alpha-helices combined were folded in four beta-strands of identical length.
- Bacteriorhodospin (Mw = 26 kDa) is a protein with purple colour. The protein acts as a light-activated proton pump that provides energy for cellular functions. The structure, revealed by both electron microscopy and X-ray crystallography, showed that the protein consists of 7 transmembrane spanning helices (TMH). Each TMH traverses the lipid bilayer completely (thickness of 45 Å). a)Calculate the minimum number of amino acid residues needed per TMH to completely cross the membrane. b)Estimate how large a fraction of the bacteriorhodopsin protein that is made up by TMHs. c)Now that you know the fraction of the protein that is made up by TMHs, at which ψ/φangles will the amino acids cluster in a Ramachandran plot?List some of the possible combinations of α-helices and βsheets in supersecondary structures.Alpha-helices have 3.6 amino acid residues per turn, ie a helix 36 amino acids long would form 10 turns, and The axial distance between adjacent residues is 3.5 Angstroms. Beta-helices have two residues per repeat unit which gives the beta-strand a 7 Angstrom pitch. This compares with the alpha-helix where the axial distance between adjacent residues is only 1.5 Angstroms. Then how many residues in an alpha-helix conformation would it take to traverse the same distance as 10 residues in beta-strand conformation?
- In a 0.1 M lysine solution, what are the individual concentrations of the protonated C-terminus form of the amino acid versus the non- protonated at pH 4 (pKa = 2.16)PfCRT is found to have 10 peaks on a hydropathy plot given its primary sequence. Researchers also noted that each peak is comprised of about 30 amino acids. The digestive vacuole membrane is 45Å in Plasmodium species. Explain why researchers conclude there are 10 transmembrane helices from these two pieces of data.Describe the general structure of a type 2 alpha helix protein. Explain how type 2 alpha helix transmembrane domains can be used to form pathways for large polar and charged molecules to traverse the lipid bilayer of the cell membrane.
- The diagram to the right illustrates the inter-actions of the amino acid side chains of two a-helical polypeptide strands in a coiled-coil, viewed end-on and projected along the helix axes from the N-terminal to the C-terminal end. Are the macrodipoles of the two a- helices oriented parallel or anti-parallel? For this projec- tion is the positive end of the macro-dipole in the sur- face of the paper or below the surface? f C b g e d a' a d' g b' f'There are different types of helical structures that can be found in proteins (i.e., not only helices). What is common among different types of helices is that the he structure is maintained by intrachain hydrogen bonding between two polypeptide backbone atoms. Oftentimes, at least two intrachain hydrogen bonds need to be formed in order for a helix to start gaining stability. This can be observed from circular dichroism, technique that detects helicity in proteins. Circular dichroism starts detecting helicity in a helical chain only when there are at least two intrachain hydrogen bond formed. If a helical structure is too short such that it only has one intrachain hydrogen bond, the helix is too unstable for the helicity to be accurately detected th circular dichroism. Four different types of helical structures were studied using circular dichroism and the minimum number of residues needed for helicity to become detectable wa determined as summarized in the table below. Minimum number…It is often the case that a helices are positioned in a protein such that one side faces the interior of the protein and the other, the surface of the protein. These are said to be amphiphilic helices because they face different environments. Using a helical wheel projection (shown below), which of the peptide(s) below might form an amphiphilic helix? 8 15 1 12 4 11 16 18 9 7 14 13 10 17 O SLIKSVIEMVDEWFRTFL O FLIRVLRKVFRVLTRILS O RLFRSRVLKIAVIRFLLI