The figure below illustrates what reactions of amino acids? coo &C=0 CH₂ CH₂ 0=( 00 + NHⓇ NAD(P)H+H NAD(P) + H₂O Coo I H₂N-C-H CH₂ I CH₂ 3=0 COOⒸ ATP ADP +P; H₂N-CH 1 NH ΝΗ, I CH₂ 1 CH₂ 0=( NH₂
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- Determine whether each of the amino acids is polar, nonpolar, positively charged, or negatively charged at pH 7. Polar and neutral aspartate H Ser H₂N-C-CH₂-C-COO NH3 lysine Leu Nonpolar Answer Bank H OOC-CH₂-CH₂-C-COO NH3 Positively charged H CH₂-C-COO NH3 hydrophobic amino acids Negatively chargedH CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln 8. How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. 9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. 12. Cyanogen bromide is a chemical reagent which also cleaves peptide bonds.…
- Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. List down the different fragments that would result if dynorphin were cleaved by trypsin. . How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. . Cyanogen bromide is a chemical reagent which also cleaves peptide bonds. What is/are…Copy of The following reaction scheme shows the states of the amino acid hisitdine. Histidine has three pKa's - 2, 6 and 9.2. Which form of Histidine predominates at pH of 5? *H3N-CH-Ĉ-OH CH2 *H3N-CH-C–O- CH2 "H3N-CH-C-O- CH2 H2N-CH-C–O- CH2 +HN *HN N' -NH -NH -NH NH A C O A. A ОВ. В OC.C O D.D O E. The answer cannot be determined with information given.Question 20 Signal sequences are often found at the C-terminus of the polypeptide chain. True False Question 21 Attachment of an isoprenid group to a protein to form a lipid-linked protein Palmitoylation Acetylation Prenylation Lipidation Question 22 Each GroEL subunit has an ATP-binding pocket that catalyzes hydrolysis of its bound ATP True False Question 23 Calnexin and calreticulin recognize lipid molecules covalently attached to proteins to assist proper folding and translocation O True O False
- QUESTION 2 Which peptide will most strongly attach to a carboxymethyl ion exchange column at pH 7.4? O N'-Glu-Lys-Arg-Asp-Tyr-C' O N'-Tyr-Arg-Lys-Arg-Gly-C' O N'-Gly-Glu-Gln-Asp-Asp-C' O N'-Val-Ala-Leu-lle-Arg-C' QUESTION 3 Which will be product of transcription from this double-stranded (ds) DNA sequence? 5' - atgttcaaagcctattcg - 3' 3' - tacaagtttcggataagc - 5' O YKFRIS O uacaaguuucggauaagc O auauucaaaaccuauuca Which will be product of transcription from this double-stranded (ds) DNA sequence? 5' - atgttcaaagcctattcg – 3' 3' - tacaagtttcggataagc – 5' O YKFRIS O uacaaguuucggauaagc O auguucaaagccuauucg Ο MFKAYS QUESTION 4 The structure of hemoglobin consists of a 2a and 2B heterotetramer. O quaternary O tertiary O secondary O primaryCalculate the net charge of the following peptide at pH 2, pH 6 and pH 14 (use 2 and 9 as pKa values for the carboxylic acid and amino groups, respectively, use the attached table for the side chain pKa values). Ile-Leu-Ile-Lys-Glu-Cys-His-Glu-Met-Ile-Ser-Thr-Arg-TyrThis is a hw question Define protein denaturation and explain its significance to metabolism( chemical reactions in cells)
- 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 bodyModern medicine now uses insulin analogues (where one or more of the amino acid residues has been changed) in the treatment of diabetes. In one such analogue, glargine insulin, the changes have increased the isoelectric point of the enzyme from 5.4 to 6.7, thereby reducing its solubility at physiological pH. Explain how changes in the primary amino acid sequence can alter the pI and solubility of the analogue without altering its interaction with blood glucose.Indicate which of the amino acid residues in the following peptide sequence contains a group that has a positive charge for its most likely charge state at pH 10. Asp-Tyr-Lys-GIn-Thr-Ile-Phe-Met-Ser (If none of the amino acids fit the criterion, select "none".) Asp Tyr ооооооооо Lys Gln Thr lle Phe Met Ser none