Which of the following correctly describes a typical alpha helix protein secondary structure?
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Q: N-terminus
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A: There is a different shape of a protein in its secondary structure.
Q: Which of the following characterize -helix regions of proteins? (A) They all have the same primary…
A: Helix is a protein structure that looks like a moving staircase or a spring. The wire of the spring…
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Q: Which of the following is a secondary protein structure? a) Ensilon turn
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Q: What is the quaternary structure of a protein? Do all proteins have quaternary structure?
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Q: A. What type of secondary structure predominates in avidin, alpha helices or beta pleated sheets?
A: Since you have asked multiple questions, we will solve the first question for you. If you want any…
Q: What type of bonds/forces stabilize protein secondary structure?
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Q: What is the tertiary structure of a protein? What are the main types of tertiary structure?
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Q: Name two(2) interactions that maintain tertiary protein structure.
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Q: Why is the 3-Dimensional structure important for protein function?
A: “Since you have asked multiple questions, we will solve the first question for you. If you want any…
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Q: The structure shown below belongs to which family of protein tertiary structure? PDB: 1Z4A 1) a/ß…
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Q: I-D-E-L-Y-S-Q-V-C-S-H-L-D-T-V-R This amino acid sequence forms an alpha helix. When thinking about…
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Q: Which of the following contribute to and/or describe protein secondary_structure? O All of the…
A: Secondary structure is defined by the regular, arrangements that recur in space of adjacent amino…
Q: Which of the following statement about proteins is correct a. alpha helix and Beta pleated sheets…
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Q: In the tertiary structure of a protein, which pair of amino acid side chains would be most likely to…
A: Introduction: Protein are the most bountiful natural particles of the living framework. They can be…
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- Consider the following protein sequence as an α helix: Leu-Lys-Arg-Ile-Val-Asp-Ile-Leu-Ser-Arg-Leu-Phe-Lys-Val. how many turns does this helix make?The domain of a protien is approximately 350 residues in length. what is length (in A°) of this domain? if this same peptide segment were a true alpha helix, how long would it be? if the same segment were beta sheet, what would its length be?Assume that the 3 polypeptide strands shown below form a parallel B-sheet. Select amino acids AA1, AA2, and AA3 so that the parallel B-sheet is amphipathic and remains stable. Glu-lle-Asn-AA1-Cys-Val Ser-AA2-GIn-Leu-Lys-Phe Lys-Met-Cys-Leu-AA3-Val O AA1 = Pro, AA2 = Leu, AA3 = lle O AA1 = Val, AA2 = Leu, AA3 = Asn O AA1 = Ala, AA2 = Gly, AA3 = Leu AA1 = Phe, AA2 = Arg, AA3 = Ala O O
- Which amino acid sequence will form part of which protein structure, and why? Sequence 1: Ser-Phe-Gln-Val-Lys-Leu-His-Tyr-Asp-Val Sequence 2: Glu-Tyr-Leu-Asn-Phe-Ala-Gln-Val-Leu-Arg __Amphipathic beta strand __ Amphipathic alpha helixThe 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'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?
- For the three peptides below, label whether they would form an amphiphilic beta-strand, amphiphilic helix, or nothing. Explain why. Part a) S-V-K-I-Q-M-R-A-D-L Part b) A-L-E-H-M-F-R-Y-L-A-K Part c) A-L-A-I-W-F-P-D-R-K-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 missenseName the protein structural element shown in yellow in the figure: B-barrel reverse turn disordered region a-helix parallel ß sheet
- Describe the structure of IgG in detail by referring to the different levels of protein structureWhich of the following sequences is most likely to represent a beta-sheet portion of a protein? -lle-Val-Thr-Thr-lle-Val- O -Lys-Lys-Lys-Lys-Lys-Lys- -Arg-Arg-Ser-Gln-Gln-Arg- O -Asn-Glu-Arg-Gln-Arg-Glu-GLUT1 is a type III integral membrane protein with 12 amphipathic helices that span the cell membrane. Which amino acid side chains from the following amino acid sequence are most likely to form the hydrophobic (non-polar) face of an amphipathic alpha helix? -Ser-Leu-Val-Thr-Asn-Phe-Ile- 094 1 Select one: 5 4 W 7 2 6 3 DRO 10:00