Which amino acid residue is most likely to be found in position "a" or "d" of the pseudo repeat in? keratin? Glu Val Lys Pro Trp 13
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- An a-Helix (or helices) is often found at anion binding sites of different proteins. Explain this observation using a schematic drawing of a-helix. Clearly indicate the direction of the dipole and the N-terminus of the helix. Show the structure of the functional group of the glutamic acid side chain in its (general) base form.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.A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown here. Only one of the Cys has a free —SH group, and the other two are involved in an —S—S— bond. The only methionine and the only aromatic amino acid (Phe) in this protein are in the positions indicated. Cleavage of the intact protein (i.e., withdisulfide bonds intact) by either cyanogen bromide or chymotrypsin does not break the protein into two peptides. Where is the —S—S— bond (i.e., AB, BC, or AC)?
- A schematic diagram of the helical structure of cytochrome b562 is reproduced below. Thisprotein belongs to the family of -proteins that have a four-helix bundle. Number the helices 1 – 4according to their N C direction. Indicate relative orientations of the macrodipoles of helices 1 – 4adjacent to the diagram of cytochrome b562. Remember that according to the definition of a dipolethat the arrow points towards the positive end.Glycosylation is a major type of protein post-translational modification. Identify the amino acid that is joined to each monosaccharide by a glycosidic bond. glycoprotein A glycoprotein B glycoprotein C HA HO Н CH₂OH HO OH Н H CH₂OH Н ОН HO HN-C-CH3 о c=0 NHI -NH-C - CH2C-H ОН Н нн ОН НН CH2OH Он OH HO Н NH 1 С=0 -CH2-C-н NH C=0 LO-CH2-C-H NH A В сTo visualize the spatial arrangement of amino acid residues in an a-helix, it is helpful to imagine you are looking down the long axis of the helix, just as you would look down a soda straw. Viewed in this orientation, the residues form a circle, with each residue offset from its neighbor by 100 degrees. This representation is called a helical wheel. Use the circle below to indicate the position of each residue around the helix of the enzyme lysozyme. NH ...Arg - Cys - Glu- Leu - Ala Ala - Ala Met-Lys COO- The first two amino acids, Arg-1 and Cys-2, are shown as an example. Arg-1 O Glu-3 Which amino acid in the polypeptide is the first to pass the origin (i.e., which amino acid passes Arg- 1 first, completing one full circle)? Select the best answer. O Leu-4 O Ala-5 O Ala-6 O Ala-7 Met-8 O Lys-9 100° O none of the above Cys-2
- Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide. I don't understand how the order of amino acids in Step 2 was arranged. Please explain. Thank you.Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide.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, a measure of a solution’s capacity to rotate circularly polarized light. Polyglutamate, a polypeptide made up of only L-Gluresidues, has the α-helix conformation at pH 3. When the pH is raised 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 the pH is lowered to 7 the specific rotation also decreases, as shown by the following graph. What is the explanation for the effect of the pH changes on the conformations of poly(Glu) and poly(Lys)? Why does the transition occur over such a narrow range of pH?
- The 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 handedGLUT 1 contains several amphipathic transmembrane hellices, each with Its polar face oriented towards the central cavity, producing a transmembrane channel available for interaction with glucose, as shown in the figure below. Which of the following sequences are most likely to form a transmembrane helix? Helical wheel diagram is given for reference. a Ser-Ala-Val-Phe-Thr-lle-Met O Phe-Leu-Val-Thr-Asn-Met-lle O Val-Ser-Thr-Val-Phe-Asn-Glu Ser-Asn-Leu-Asp-Gin-lle-Phe O Asn-Leu-Ala-Ser-Gin-Phe-eChanging one amino acid within a protein sequence from a tryptophan to a stop codon would be best classified as Amino acids groups Group Characteristics Names Ala, Val, Leu, Ile, Pro, Phe Trp, Met Ala: A Leu: L non-polar hydrophobic Arg: R Asn: N Lys: K Met: M Asp: D Cys: C Gly: G polar hydrophilic (non-charged) Gly , Ser, Thr, Cys, Tyr, Asn Gln Phe: F Pro: P Ser: S acidic negatively charged Asp, Glu Glu: E Gln: Q Thr: T His: H lle: I Trp: W Туr: Y Val: V basic positively charged Lys, Arg, His A) Conservative missense O B) Nonsense O C) Neutral O D) Non-conservative missense