Name Lysine Arginine Histidine Aspartate Glutamate Structure 1-Let Abbr 3-Let Abbr Class Special Props рка Side Chain
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For each amino acid, show the structure, 1-letter abbreviation, 3-letter abbreviation, class (non-polar, polar, positive or negative), special props, side chain pKa)
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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 body0ミレーNレ NH geometry on both cand N. Torigonal plannes CH - C-N o=), HN CH2 CH-C-OH (a- carbon) CH2 HooC Aspaxagine - Toline - Valine - Arginine - phenylalcmine - Glutamic ocid. 1.Give the name and three letter code for each amino acid in the peptide. e 2. At pH 7, approximately what charge would be on your peptide? Explain your answer. 3. Can your peptide form intra/interchain disulfide bonds? Explain why/why not. e 4. Will your peptide absorb UV and is it fluorescent? Explain why/why not. e 5. What is the probability that your peptide contains a cis peptide bond? Explain your answer.wnich snows tne specinicity pockets. The S pocket nas a Ra glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S,' pocket is deep and hydrophobic. Suggest a 3-amino acid sequence that this protease would R2 H cleave and indicate between which sites the peptide bond would be broken. S2 Which sequence would this protease cleave? Val-Lys-Phe Phe-Lys-Val Lys-Phe-Val Val-Phe-Lys Phe-Val-Lys O Lys-Val-Phe The peptide bond that is broken is between which sites? O S2 and S,' OS, and S,' O S2 and S1 O S2 and S1, and S and S,' IZ
- . The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme C would result in exces- sive urinary excretion of what compound?A Classwork for BTMF_Itani_ Biolo x A S'ERRA STANLEY -protein-synth X O 8 period light reaction - Google S x google.com/document/d/1plhyciPrM-AMsQKmaUHZSZU44EJL85jDuCyDxE01E60/edit - protein-synthesis-worksheet_practice-converted O sert Format Tools Add-ons Help TUR Last edit was 10 minutes ago 0% Normal text Noto Sans BIUA 川。 三E▼=、三三 13 + 田回▼ 1 3 4. 5 8. DNA → TAC AGA CGG CAA CTC TGG GTG CTT TGT TCT CTT CTC AGT ATC mRNA → protein > Son out Co 4. 6. 8. 9.The glycosaminoglycan polysaccharide chainsthat are linked to specific core proteins to form the pro-teoglycan components of the extracellular space arehighly negatively charged. How do you suppose thesenegatively charged polysaccharide chains help to estab-lish a hydrated gel-like environment around the cell? Howwould the properties of these molecules differ if the poly-saccharide chains were uncharged?
- Treatment of a polypeptide with 2-mercaptoethanol yields two polypeptides 1. Ile—Val—Cys—Arg—Thr—Gly—Cys—Lys—Asn—Phe—Leu2. Trp—Lys—Cys—Phe—Arg—His—Thr—Lys—Cys—SerTreatment of the intact polypeptide with trypsin yields fragments with the following aminoacid compositions(Arg, Cys2, Ile, Ser, Val)(Arg, Cys2, Gly, Lys, Thr, Phe)(Asn, Leu, Phe)(His, Lys, Thr)(Lys, Trp)Edmands chemistry reveal the following PTH derivatives in equal quantity after cycle 1• PTH--Ile and PTH--Trp a) Rewrite the intact polypeptide, by indicating the positions of the disulfide bonds(Indicate your reasoning) b) How many products do you expect after chymotrypsin cleavage of the intactpolypeptide? c) You are performing an isoelectric focusing experiment (IEF) on a gel with a pH range of 2to 14. Indicate on the diagram below at what point along the gel will peptide 1 abovefocus, in the presence (X) and absence (Y) of DTT. (also show your calculations)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 chargedOne round of Edman degradation of the peptide: H2N- Gly-Arg-Lys- Phe-Asp- COOH which of the following structures would result when add cyanogen bromide ? A) H2N-Gly-Arg-COOH + H2N–Lys-Phe- Asp-COOH B) H2N-Arg-Lys-Phe-Asp-C0OH+ Gly C) H2N- Gly-Arg-Lys-Phe-Asp- COOH D) H2N-Gly-Arg-Lys-Phe-COOH + Asp E) H2N-Gly-Arg-Lys-COOH + H2N-Phe-Asp-COOH
- cip sequence rule in ephedrineUpload a drawing of Gly-Met-Asn-Glu-His Label the alpha carbons Label the R groups as hydrophobic or hydrophilic Label the acidic and basic R-groups Label the peptide bonds Label the N terminus and the C terminusThesecondarystructureofaproteinisinfluencedbybothhydrogen bonding and London dispersion forces. a. Usingastructuralformula,showanexampleofhydrogenbonding between the serine portion of a protein and the tyrosine portion b. Usingastructuralformula,showanexampleofLondondispersionforces between the leucine portion of a protein and the valine portion