results from hydrogen bonding between the backbone constituents of the overall shape of a polypeptide the polypeptide primary structure the aggregation of multiple polypeptide subunits secondary structure B pleated sheet results from interactions between side chains (R groups) of amino acids a helix tertiary structure amino acid sequence quaternary structure
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- pQLSeysIVg8-5-v0riWm3uEQ4RUA3Hdua_NDMQI25SST619X-KVA/viewform What makes alanine a nonpolar, neutral amino acid? O The presence of a chiral carbon O The hydrocarbon group attached O The zwitterion cannot be formed due to nonpolarity O The acid and base groups neutralizes the side chains What is NOT true about hemoglobin? It is a fibrous protein that helps oxygen combine with carbon It has an iron atom inside the structure It contains four polypeptide units O It transports oxygen to the different cells in the bodyAmino Acids Cys A lanine CH2 SH Leucine Isoleucine Leu Ser As partil acia Gly Sev Leu Serine Isolcucne valine -citz pn Val CHziPr -Me Asparti -CH2 SH -CH2 Ph Acid pnerinl Esoleucine alanine Gly Ala Glycine 1 Alanine А Ala -Me 2 Cysteine C Сys -CH,SH 3 Phenyl alanine F Phe -CH,Ph 4 Leucine L Leu -CH,iPr 5 Aвpartic Acid D Asp -CH,CO,H Glycine Gly -H Serine Ser -CH¿OH 8 Valine V Val -CH(Me); 9. Isoleucine Ile -CH(Me)EtAla Leu Glu Glu Asn Ala represent the following amino acid in its predominant form at pH= 7
- Examine the peptide. Thr‑Lys‑Pro‑Ile‑Val‑Ala‑Pro‑Met‑Glu‑Tyr‑Gly‑LysThr‑Lys‑Pro‑Ile‑Val‑Ala‑Pro‑Met‑Glu‑Tyr‑Gly‑Lys Write the sequence using one‑letter abbreviations. Estimate the net charge on the peptide at pH 7. Estimate the net charge on the peptide at pH 12.A peptide has the sequence Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–GlyGlu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly The p?apKa values for the peptide’s side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side‑chain pKa glutamate 9.609.60 2.342.34 4.254.25 histidine 9.179.17 1.821.82 6.006.00 tryptophan 9.399.39 2.382.38 serine 9.159.15 2.212.21 glycine 9.609.60 2.342.34 leucine 9.609.60 2.362.36 arginine 9.049.04 2.172.17 12.4812.48 proline 10.9610.96 1.991.99 Calculate the net charge of the molecule at pH 3.Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU I NEED IT ASAP PLEASE
- A peptide has the sequence Glu-His–Trp–Ser-Gly–Leu-Arg-Pro–Gly The pK, values for the peptide's side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side-chain pKa glutamate 9.60 2.34 4.25 histidine 9.17 1.82 6.00 tryptophan 9.39 2.38 serine 9.15 2.21 glycine 9.60 2.34 leucine 9.60 2.36 arginine 9.04 2.17 12.48 proline 10.96 1.99 Calculate the net charge of the molecule at pH 3. net charge at pH 3:s) This is a Fish er projecti on of D-f ructose (Fisher projecti on of L-F ructose ). Dra w L-fructose. Inaddition, draw the Haworth projection of a-D fructofuranose and b-D fructofuranose, the cyclic form ofthis monosaccharide. Draw sucrose where indicated below (Haworth projection).unu meleDy aln ncease In BIUUU giucose concentration. In the absence of glucose, cells rely on fats as a source of energy. 1. Protein Structure and Chemistry The primary structure of human insulin is shown below. It is made up of two polypeptide chains that come together in a quaternary structure. The first amino acid of each chain islabeled with the number 1. A handout with all amino acids and their structure and properties is provided on page 5. Primary structure of proteins 1a. Circle and label the amino and carboxyl ends in the primary structure of each polypeptide. Draw the appropriate functional groups at each end. Ceu Ala 1b. Identify and label one amino acid each with side groups that are: i) polar ii) non polar iii) acidic iv) basic Glu Chain B 30 amino acids His Secondary structure 1c. Show one H-bond that determines the secondary structure of the protein. You should indicate the bond in the diagram using appropriate functional groups. Gin Cya Chain A 21 amino acids Thr Gin…
- N- HO sta on e yor current pH the peptide? Explain your yor a) Based the charge state shown, what is a possible vahe amswer wsi'ng 2-3 sentences. Show the qull pH ramge yor this protonation otate 6) Hypo thesize a oingle amino acid substitution Cmutation) that wonld make Your amswer must include the which residue this lic You. peptide more hydrophi you would mutate and what new re sidue would take its place Include a 1 sentence explanation g your reasoning yourAmino Acid 3-Letter 1-Letter Second letter Code Code Alanine Cysteine Aspartic acid or aspartate Glutamic acid or glutamate | Phenylalanine Glycine Histidine Ala Cys Asp Glu UCU Phe UGU cys UGC UUUT UAU Tyr UAC D UUC UC Ser UUA UAA Stop UGA Stop UAG Stop UGG Trp G UCA Phe Leu UUG UCG Gly G H. His Ile CUU CCU CAU CGU U His CAC CÚC Leu CUA CGC CGA Isoleucine Lysine Leucine Pro Arg Lys K CAA Gin CAG CCA Leu L. CUG CCG CG Methionine Met M AUU AUC le ACU) ACC AAU1 AAC AGU Asn Asparagine Proline Glutamine Arginine Serine Asn Ser AGC AGA Arg Pro P. Thr AAA Gln Arg Ser AUA ACA AUG Met ACG AAG Lys AGG R GUU) GCU) GAU1 GGU GGC Gly Threonine Valine Tryptophan Tyrosine Thr GUC Val GUA GCC Ala GCA Val V GAA GAG GGA W Trp Тут Glu GUG GCG GGG Y Apply all that you have learned to solve the following: If you have the following DNA sequence: 5-ATGGCIOTOGTATTAAATAG-3 1. What is the sequence of the bases in the complementary DNA strand in a 3' to 5 direction ?( NB" Just type the letter for the bases) 2.…NAZO NHZ Ala-Cys-Glu -Tyr - Trp - Lys - Arg - His -Pro-G ly Glu pka 4.15 SH Tyr 10.10 Draw Charges Lys 10.67 Olt A3 12.10 +NH₂ Ntrm 2) Calculate net charge 3) write out I letter code 300 Ctim 3 juli of peptich (above) Ⓒ pH; 1,7,12