3. Below is a polypeptide with an unknown number of amino acids. On the diagram below: a. Circle EVERY peptide bond b. Circle and number each amino acid from 1, 2, 3, and so on; from left to right c. Label each amino acid as polar, non-polar, or electrically charged d. Label the N-terminus and C-terminus e. Select three pairs of amino acids that could potentially interact to influence tertiary structure AND state the bond/force/interaction type involved in each pair. H₂N- I CH3 O HHO || -N-C-C I CH₂ OH HH OHH OHH OHH OHH OHH OHH I || ! || | || | || | N-C-C-N-Ć-T N-C-C-N-C-C-N-C-c- -C-1 | CH₂ CH₂ CH₂ CH₂ CH₂ -NH SH G SA X T H₂N H₂C I CH CH3 H
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- On 4. Below is a polypeptide with an unknown number of amino acids. On the diagram below: a. Circle EVERY peptide bond b. Circle and number each amino acid from 1, 2, 3, and so on; from left to right c. Label each amino acid as polar, non-polar, or electrically charged d. Label the N-terminus and C-terminus e. Select three pairs of amino acids that could potentially interact to influence tertiary structure AND state the bond/force/interaction type involved in each pair. H₂N-CH-C-N-CH-C- CH₂ CH₂ CH₂ NH CINH NH₂ Accessibility: Investigate CH₂ -NH -CH-C-N- CH-OH CH3 -CH-C-N CH₂ CH₂ -N- OH CHIC-OH CH₂ OH2. Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show in zig-zag style, from amino to carboxy terminus, with correct stereochemistry a. Draw the predominant form at pH = 2 b. Draw the predominant form at pH = 5 c. Draw the predominant form at pH = 7 d. Draw the predominant form at pH = 121. Hydrogen bonds can form an alpha helix or beta sheet. The hydrogen atom has a partial positive because of the atom it is covalently bound to. Name the two most common atoms hydrogen bonds within biological systems that give hydrogen a partial positive charge. 2. Are the atoms named in the question above in the backbone of the protein or are they found in R groups? Which R groups? 3. Besides hydrogen, what other atom is involved in the hydrogen bonds in an alpha helix or beta sheet? In other words, hydrogen is interacting with what other atoms when it makes a hydrogen bond? 4. Write out, in order, the full names of the seven amino acids circled in the picture.
- Draw at least 2 amino acids. Label the N-terminus and the C-terminus. Describe the property of the amino acids.1. (4) Explain the following observation: At a pH of 7:0, polylysine, which is a peptide in which all the residues are lysine, adopts a random coil. At a pH of 12.0 it adopts a helical structure.7. A peptide has the sequence Cys-His-Glu-Met-lle-Ser-Thr a. Write out the single letter sequence of this peptide. b. What is the overall charge of the peptide? Is it acidic? Basic? c. Draw the chemical structure of the peptide at pH 7.0 and show any charged groups d. What is the classification of each amino acid in this peptide regarding polarity and charge? 8. The following proteins represent a wide range of molecular weights and isoelectricpoints. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at phH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated…
- 1. a. Draw the following pentapeptide: lysine-leucine-aspartate-threonine-phenylalanine b. Label the amino and carboxyl terminus of your peptide c. Label each amino acid residue with one and three letter abbreviations d. Label the alpha carbons e. Label the bonds around which phi and psi rotational angles occur f. Which amino acid in this chain is most likely to be phosphorylated? Which amino acid is most likely to be acetylated?1. Draw (or insert) the general formula of an amino acid and label the four components. Which one gives the molecule its functional role? 2. What determines the three-dimensional structure a protein will have in the cell? 3. How is the structure of a protein related to its function in the cell? Be specific and give an example.Label: 1) the type of chemical bonds between the amino acids (e.g. covalent bond, ionic bond, metallic bond) 2) the type of interparticle forces of attraction occurring within the protein and with its environment *Indicate at least four observed interparticle forces of attraction *pink - negatively charged, blue - positively charged, yellow - nonpolar and uncharged, green - polar and uncharged *[See example picture] The chemical bond (shown by the arrow) is depicted as a line between the amino acids. Interparticle forces of attraction, such as the one between Phe and Glu (boxed), are not represented by lines but rather by the proximity of amino acids.
- Refer to the figure below, what are the following forces of attraction is involved in the protein folding for each number. 1. 2. CH₂ C-OH CH₂ 3. 4. CH H₂C CHS H₂C CH3 CH CH₂-S S-CH₂ 3 –CH,CH,CH, CH, NHA peptide has the sequence Gly-Ser-Lys-Ala-Gly-Gly-Arg-Ser-Arg. How many fragments would result from cleaving the sequence with trypsin? number of fragments: 3 Draw the smallest fragment at pH 7. + H₂N H O OH ZH N O _.. NH ₂Please describe what is a peptide bond? What is the significance of the amino terminus versus the carboxy terminus? At which end are amino acids added to form a polypeptide, this is the term for linked amino acids? What are the 3 chemical groups that form an amino acid? A▾ B I I @ & 7