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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- Changing 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 missenseThe 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'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 correct
- Do not copy anywhereOne common secondary structure found in proteins in the a-helix. On the diagram below is an a- helical region of the enzyme lysozyme. The sequence of this region is: NH Arg - Cys - Glu - Leu - Ala-Ala-Ala-Met-Lys. COO- 0 0 on the top 0 on the bottom R Is the N-terminus on the top or on the bottom of this diagram? RWhat is a helix-turn-helix motif? secondary structure in which an α helix is separated from a β sheet by a loop supersecondary structure in which an α helix is separated from another α helix by a turn supersecondary structure in which a β sheet is separated from a helix by a turn secondary structure in which two right-handed α helices are intertwined secondary structure in which two left-handed α helices are intertwined
- 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 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 helixConsider 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.Which amino acid residue is preferred at which position in the following peptide for cleavage by cyanogen bromide (CNBr)? methionine at R2 lysine at R1 methionine at R1 lysine at R2