An a helix would be destabilized MOST by ○ a glycine residue adopting alpha-helical backbone dihedral angles ○ interactions between neighboring Asp and Arg residues ○ interactions between two adjacent hydrophobic Val residues O the presence of an Arg residue near the carboxyl terminus of the a helix O the presence of two Lys residues near the amino terminus of the a helix
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- Long-range interactions between residues on a single polypeptide chain are classified as quaternary structures. On the other hand, interactions between residues on separate polypeptide chains are classified as tertiary structures. O Both statements are correct O The first statement is correct while the second statement is incorrect O Both statements are incorrect O The first statement is incorrect while the second statement is correctThe pi-helix is a rare secondary structural element in proteins that resembles an alpha helix but has slightly different properties. Notably, hydrogen bonds within a pi-helix display a repeating pattern in which the backbone C=O of residue i hydrogen bonds to the backbone HN of residue i+5. Based on this information, which of the following are true? Select all that apply. O The hydrogen bonding distance between C=O and NH groups remains unchanged between pi-helices and alpha-helices The torsion angles of amino acids found in pi-helices are the same as those found in alpha-helices Pi-helices have a smaller rise per residue compared to alpha- helices Pi-helices have fewer residues per turn compared to alpha-helices Pi-helices have more residues per tůrn compared to alpha-helices Pi-helices are left handedShow below is a polypeptide comprised of 3 α-helices and 5 β-sheets joined by randomcoil. Characterizetheforces that stabilize the tertiarystructure and draw the interacting side chains ofd) Cys Cys
- A helical wheel is a two-dimensional representation of a helix, a view along its central axis. Label the blanks on the helical wheel diagram to show the distribution of amino acid residues in a helical segment with the sequence -Val-Asp-Arg-Val-Phe-Ser-Asn-Val-Cys-Thr-His-Leu-Lys–Thr-Leu-Gln-Asp-Lys- 1 Answer Bank H L D K R F T K S TWhich of the following is the TRUE statement? When found together, a helices and B sheets are generally found in the same structural 'layer The B conformation is most stable when the individual segments are twisted in a left-handed direction Hydrophobic interactions make a large contribution to the stability of protein structures, therefor, burial of hydrophobic amino acid residues need at least two layers of secondary structure The backbone segment of a ß conformation polypeptide segment can readily H-bond to an a helix adjacent to itConsider the hydrogen bonding pattern of an a-helix with the following sequence: Asparagine's carbonyl oxygen is hydrogen bonded to: Lysine's backbone amide hydrogen O a Ob Aspartate's backbone carbonyl oxygen Oc. Tyrosine's backbone amide hydrogen Serine's backbone amide hydrogen Od Leucine's side chain Oe. DLRANGCTSY
- Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.Given the structures of the ribonucleotides as (shown in Image A) and deoxyribonucleotides (as shown in Image B), Draw the structure of the polyribonucleotide UAGCCUG and the structure of thepolydeoxyribonucleotide CGTAGAT.Glutamine is a conservative replacement for asparagine in the primary structure of a protein. This implies that
- wnich snows tne specinicity pockets. The S pocket nas a Ra glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S,' pocket is deep and hydrophobic. Suggest a 3-amino acid sequence that this protease would R2 H cleave and indicate between which sites the peptide bond would be broken. S2 Which sequence would this protease cleave? Val-Lys-Phe Phe-Lys-Val Lys-Phe-Val Val-Phe-Lys Phe-Val-Lys O Lys-Val-Phe The peptide bond that is broken is between which sites? O S2 and S,' OS, and S,' O S2 and S1 O S2 and S1, and S and S,' IZSpecific rotation is a measure of a solution's capacity to rotate circularly polarized light. The unfolding of the α helix of a polypeptide to a randomly coiled conformation is accompanied by a large decrease in a property called specific rotation. Polyglutamate, a polypeptide made up of only l-Glu residues, is an α helix at pH 3. When researchers raise the pH to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (l-Lys residues) is an α helix at pH 10, but when researchers lower the pH to 7, the specific rotation also decreases, as shown in the graph. The graph plots pH on the horizontal axis ranging from 0 to 14, labeled in increments of 2, against specific rotation on the vertical axis. The curve for poly (Lys) begins as a horizontal line just above the horizontal axis. This is labeled, random conformation. At 8.5, it bends sharply upward and becomes diagonal at 8.8 until 9.9, when it reaches a height of two-thirds of the height of the…A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis. From this information, deduce the primary structure of this polypep- tide. Fragments are grouped according to size. Pentapeptide Fragments Tetrapeptide Fragments Phe-Val-Asn-Gln-His Gln-His-Leu-Cys His-Leu-Cys-Gly-Ser His-Leu-Val-Glu Gly-Ser-His-Leu-Val Leu-Val-Glu-Ala
