Name the peptide * он H,'N-CH-C-N-CH-C-N-CH-C-O CH, CH-CH, CH, H он H. CH, CH, CH, SH CH, Methionyl-leucynyl-cycteine O Methionyl-leucinyl-cycteine O Leucyl-methionyl-cycteinyl O Methionyl-leucyl-cysteine
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- After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?Write the name of the oligopeptide L-E-T-S-P-R-A-Y using their full amino acid names. Draw the structure of olgopeptide L-E-T-S-P-R-A-Y.First letter U C A UUU UU JUC UUA UUG CUU CUC CUA CUG AUU AUC AUA AUG GUU GUC GUA GUG ] Phenylalanine UCU (Phe) UCC UCA UCG Leucine (Leu) Leucine (Leu) Isoleucine (Ile) Methionine (Met) Valine (Val) CCU CCC CCA CCG b) lysine c) methionine d) tryptophan ACU ACC ACA ACG GCU GCC GCA GCG C Second letter Serine (Ser) Proline (Pro) Threonine (Thr) Alanine (Ala) UAU UAC UAA UAG CAU CAC CAA CAG AAU AAC AAA AAG GAU GAC GAA GAG ] Tyrosine (Tyr) Stop Stop Histidine (His) Glutamine (Gln) Asparagine (Asn) Lysine (Lys) Aspartic acid (Asp) Glutamic acid (Glu) UGU UGC UGA Stop UGG Tryptophan (Trp) CGU CGC CGA CGG AGU AGC AGA AGG GGU GGC GGA GGG ] 1. List the mRNA base codons for the amino acids listed below. 2. a) aspartate: Cysteine (Cys) Serine (Ser) U C Arginine (Arg) A G Arginine (Arg) U C Glycine (Gly) A G U C A G U MCAG А
- The anomer of a-D-glucopyranose is CH:OH он ÓH CH2OH он он он он CH,OH он он он он CH,OH он OH он ÓH ÇH;OH он он он онAfter a polypeptide chain has been synthesized, certain amino acids in the peptide may become modified. For each modified amino acid, identify the standard amino acid from which it is derived. Enter the unabbreviated name of the standard amino acid. OH I *NH,CH,–C–CH,CH,—CH–COO H C *NH₂ standard amino acid: Identify the modification that yields the first amino acid depicted. addition of a hydroxyl group addition of an amino group modification of the existing amino group modification of the existing hydroxyl group elongation of the side chain by the addition of a -CH₂- groupgal(a1→6)gal(a1→6)glc(a1→2B)fru. Which of the complete IUPAC of this tetrasaccharide? a-D-galactopyranosyl-(1→6)-ß-D-galactopyranosyl-(1→6)- a-D-glucopyranosyl-(1→2)-B-fructofuranose a-D-galactopyranosyl-(1→6)- a-D-galactopyranosyl-(1→6)- a-D-glucopyranosyl-(1→2)-ß-fructofuranoside a-D-galactopyranosyl-(1→6)- a-D-galactopyranosyl-(1→6)- a-D-glucopyranosyl-(1<→2)-ß-fructofuranose a-D-galactopyranosyl-(1→6)-B-D-galactopyranosyl-(1→6)- a-D-glucopyranosyl-(1→2)-ß-fructofuranoside
- 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 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.…Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEUIdentify the structure of O-a-D-sorbopyranosyl-(24)-B-D-glucopyranose below. The following structures will help: НО Н ОН х Н H H D-sorbose Н OH CH₂OH Н Н Н OH HO Н H HO H н HO ОН Н н Н О ОН O H Н CH₂OH OH OH н 0 CH2OH Н OH Н H OH Н CH₂OH H ОН Н OH Н Н Н РО OH Н HO OH н н -O CH2O Н O H H OH н Н OH CH₂OH о CHOH H H Н Ко OH H OH Н Н OH Н OH Н OH Н CH₂OH -OCHOH H OH O CH OH Н OH Н Н CH₂OH ОН он OH OH H OH H O OH CH₂OH OH ОН Н O OH OH D-glucose Н ОН Н ОН ОН
- Consider the following two peptides: I. N-Pro-Pro - Glu - Glu - Tyr - His - Cys - Ala - Glu - Gln - Lys - Leu - Ser - Ser - Phe-Leu- Thr - C II. N-Pro-Pro - Lys - Arg - Gly - Tyr - His - Gly - Glu - Asp - Glu - Asp - Glu - Ser - Gly-Phe- Tyr-C Give three reasons why_peptide I is more likely to form an alpha helix in aqueous solution at pH 7.0. Your reasons may include why_peptide Il is less likely to form an alpha helixThe melanocyte-stimulating hormone a-melanotropin has the following sequence: Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val In the one-letter code of amino acids, this sequence would be: SYSMEHFRWGKPV STSMGHFAWGKPV O SYSMDHFAWGKPV O SYSMEHFAWGLPVThe peptide cys-leu-glu-ala-cys-lys is at pH 7 in oxidizing conditions. Part a) Draw the peptide's titration curve. Part b) What would the pI of the peptide be around?