Explain the Titration Curve of Lysine
Q: Draw the zwitterion for the amino acid backbone of: glycine alanine proline
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Q: Draw a tripeptide only containing Alanine
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Q: Write structural formulas for the two dipeptides that contain leucine and aspartate.
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Q: amino acid in the form of a "phenylthiohydantoin" (PTH-amino acid), are shown below. What is the…
A: Phenyl isothiocynate is the Edman reagent. It reacts with N-terminal amino acid to give phenyl…
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A: Introduction: Talose is an aldohexose sugar that is a C-2 epimer of galactose and a C-4 epimer of…
Q: Sketch out a structure of tyrosyl-glycyl-lysine at a pH of 13
A: Amino acids are the monomeric unit of polypeptides that give proteins. There are 20 amino acids that…
Q: Explain the Titrimetric profile of Lysine in figure 2
A: The isoelectric point is the pH at which any amino acid or protein has no net charge and thus will…
Q: Calculate the pI for the following tri-peptide: Glu-Arg-Lys
A: pI or isoelectric point is the pH at which a peptide or molecule is electrically neutral. The pH of…
Q: Name the following nucleotide: HN P-0-P-0-CH2 OH
A: Nucleic acids are macromolecules. These are of two types - Deoxyribonucleic acid (DNA) and…
Q: The pH at which the Lysine R-group is 20 % dissociated is:
A: Option a) is correct Answer
Q: Draw all the possible tripeptides of serine, methionine, and glycine and name them.
A: The peptides that are made up of three amino acid sequence are termed tripeptides. These amino acids…
Q: What is the name of this tripeptide, using the three-letter amino acid abbreviations? Capitalize the…
A: Peptide or protein sequence is a linear chain of amino acids. There are 20 main different types of…
Q: Discuss the absorption spectra of arginine
A: Absorption spectra were recorded covering wavelength range 200-900 nm using ultraviolet-visible…
Q: draw a peptide bond of: glycine alanine proline
A: The amino acids are the monomers for the protein chains. The amino acid has a chiral carbon attach…
Q: Draw the structure of the α-keto acid formed by the transamination of each amino acid: (a) tyrosine;…
A: (a) Tyrosine : It is an amino acid that is naturally produced in the body from another amino acid…
Q: Given a primer sequence 3’- CTGGGAAACATTCTGGAT - 5’, compute for the melting temperature of this…
A: Melting temperature of primer can be defined as a temperature at which one half of the DNA double…
Q: Explain the Titration profile of Lysine
A: Titration is a basic process which is used to analyse a sample. It is basically used to determine…
Q: Two amino acids are each specified only by a single triplet. Identify these two amino acids and the…
A: A specific sequence of three consecutive nucleotides that is part of the genetic code and that…
Q: If guanine, found in the first base triplet, is removed, explain how this would affect the structure…
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Q: discuss the absorption spectra of the 3 amino acids Arginine, Leucine and Proline.
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Q: Define ε-amino group
A: The amino group is the -NH2 substituent in a carboxyl group. Amino groups are components of amino…
Q: Identify if the statement is correct or incorrect, "Nucleotides consist of a nitrogenous base bound…
A: The nucleotide is the smallest entity that makes up the polymers such as DNA and RNA. DNA functions…
Q: Describe lysine degradation.
A: The amino acid is an organic acid that contains an alpha carboxyl group, alpha amino group, a…
Q: Draw the dipeptide alanylvaline
A: Introduction Amino acids are organic compounds that contain the functional groups amino (–NH2) and…
Q: raw the complete structure of the tetrapeptide Val-Cys-Glu-Ser.
A: A peptide molecule is the sequence of an amino acid that is involved in the formation of a peptide…
Q: Nucleotides containing ribose, thymine, and phosphate are not found in ribonucleic acids. Explain…
A: RNA consists of ribonucleic acid, which exhibit ribose, and nitrogenous bases.
Q: Draw the α-l-glucopyranose sugars using Haworth projections:
A: α-l-glucopyranose is also known as α-l-glucose, which has the alpha configuration at the anomeric…
Q: Give the correct name for the tripeptide
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Q: The anomer of a-D-gluсоруranose IS CH2OH он ÓH он CH:OH он он он он CH,OH он он
A: Glucose is the primary source of energy for humans and other organisms as well. Glucose contain four…
Q: Arginine exists in two high-pH forms instead of the usual one. Explain why.
A: Amino acids are compounds containing carbon, hydrogen, oxygen and nitrogen. They are monomers…
Q: There are a total of six different amino acid sequences for a tripeptide containing one molecule…
A: Any peptide that is obtained by a set of three amino acids joined together is known as a tripeptide.…
Q: Define polypeptide
A: Polypeptides are short chains of between two and fifty amino acids, linked by peptide bonds. Chains…
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A:
Q: Explain about the four deoxyribonucleoside triphosphates ?
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Q: Given the polypeptide chain below: Ala-Arg-Val-His-Asp-Gln 1. What kind of polypeptide is it? 2.…
A: The organic molecule is comprised of two functional groups that are an amino group and the carboxyl…
Q: HN H H H H H Se он
A: Peptides or proteins are composed of twenty standard amino acids attached together via peptide…
Q: Draw the titration curves for the following AA’s: Aspartic acid, Alanine, Lysine, Valine, Serine,…
A: Hi! Thank you for the question. As you have posted a question with multiple subparts, I will be…
Q: NH2 N- но-Р-О 'N' ОН ОН ОН
A: A is incorrect. Reason : Adenosine does not have any phosphate group in it's structure.
Q: Draw the resulting structure if Tyr were to form an O-linkage with position 4 on B- D-fructose. Use…
A: Howarth projections of compounds gives the conformational identify of the groups that makes up that…
Q: Drew the peptide sequence and write its full name Cys-Gln-Lys-His-Ala-Ser-Gln
A: All the amino acids mentioned in the question are linked Together by peptide bonds that is CONH. A…
Q: Draw the Titrimetric profile of Lysine
A: Lysine is one of 10 essential amino acids. It is a linear, positively-charged amino acid.
Q: Would the tetrapeptide W-X-Y-Z have the same pl as a peptide Z-Y-X-W? Why or why not?
A: The isoelectric point is the pH at which any molecule (here it would be the amino acids) carries no…
Q: с" CH2 CH2 "НaN H с. CH С" CH Нзс CHз ZI о-о
A: The second amino acid in the given dipeptide is glutamate. It contains a negatively charged side…
Q: Draw the peptide formed between asparagine and histidine. H,N-CH-ċ-OH H,N- -CH—С—он CH2 ČH2 N° NH2…
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Q: Explain why Proline is seen as an exception when a ninhydrin complex is formed.
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Q: Discuss the potential difficulties of designing a diet to alleviate the symptoms of phenylketonuria.
A: Phenylketonuria is an inborn, autosomal recessive disorder that effects metabolism. The individuals…
Q: Spell out the name of the polypeptide using three letter codes for each amino acid separated with…
A: Phenyl isothiocynate is the Edman reagent. It reacts with N-terminal amino acid to give phenyl…
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- An Fab fragment binds to lysozyme with a dissociation constant of Ka = 10-11 M. A 1 nM (10-9 M) solution of lysozyme is treated with increasing concentrations of the Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to the Fab? [Fab] 9.9 Incorrect nMConsider the following protein mixture: Protein A B C D Molecular Weight (kDa) 50 150 200 350 Affinity to Metal ion === Zn²+ === 1. Using hydrophobic interaction chromatography, the protein that will be eluted last is [Select] 2. Using affinity chromatography, the protein that will be eluted last in a Zn²+-containing column is 3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select] IpH value 7 3 9 5 [Select] [Select] 4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is 5. The protein that will be eluted last in a gel filtration column is [Select] 6. Using isoelectric focusing, the protein that will have a protein band nearest to the cathode (negative electrode) is [Select] % Hydrophobicity 20 45 75 55The ESI-MS spectrum in positive ionization mode for lysozyme is obtained. a. What is the molecular weight of the protein to 5 significant figures based on the two highlighted ion species? b. What is the charge of the peaks at 1101.5 and 1789.2.
- The isoelectric point, pI, of the protein deoxyribonuclease I is 10.2 , while that of pepsin is 1. What is the net charge of deoxyribonuclease I at pH 7.3 ? What is the net charge of pepsin at pH 3.5 ? The isoelectric point of tryptophan is 5.89 ; phenylalanine , 5.48 . During paper electrophoresis at pH 6.5 , toward which clectrode does tryptophan migrate? During paper electrophoresis at pH 4.5, toward which electrode does phenylalanine migrate? [A tetrapeptide, glutamate-glycine-alanine-lysine, is prepared at at concentration of 1 mM (0.001 M) and is measured in the standard setup (pathlength of 1 cm). What is the approximate absorbance of this peptide at 280 nm? Hint: if the peptide contained a single tryptophan, the answer would be about 10. 10 280 1 0Which of the peptide sequences below best matches the hydropathy plot shown? 5 10 15 Residue Number ILYYAGSREDHSGYLIL EQSDTERNQHGALIYLI LIFLAIFPAGSTSEDRR RAFLILFMTYFLILFLI LHGDQNRERDGHSQERD 2 Hydropathy value 0 -4 -2
- Which of the peptide sequences below best matches the hydropathy plot shown? L 10 Residue Number 4 2 Hydropathy value -2 0 セー RAFLILFMTYFLILFLI ILYYAGSREDHSGYLIL OLHGDQNRERDGHSQERD EQSDTERNQHGALIYLI 01 5 154.08 2.54 H H 1.02 1.02 1.67 E E = EXON = INTRON E 10.8 kbp 3.94 3.66 E = EcoRI site wwwwwwwww H = Hindill site HI Н 10.31t E E 1.76 1.10 Note: Fragment sizes are not to scale and all fragment lengths are in kilobase pairs (kbp) The a. Indicate what enzymes you would use for digestion and the gel electrophoresis pattern of the restriction fragments (draw a diagram of the gel with fragment positions, indicate field polarity, and direction of migration). Please do single and a double digest of the DNA. GrammarlyA mixture of Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74), Phenylalanine (pl 5.48) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2. v First 1. Aspartic Acid v Second 2. Histidine v Third 3. Lysine 4. Phenylalanine v Fourth 5. Threonine v Fifth 6. No separation
- Purification of a protein of unknown structure has been achieved. The natural protein has a molecular weight of 240,000, according to size-exclusion chromatography. Using a concentration of 6 M guanidine hydrochloride in the chromatography, a single peak can be identified as the molecular weight (MW) 60,000 of a protein. B-mercaptoethanol (BME) and guanidine hydrochloride (GHC) are used in tandem to produce proteins with mass masses of 34,000 and 26,000, respectively. The structure of this protein can be inferred from these facts.TABLE 3-1 Properties and Conventions Associated with the Amino Acids pk, values Amino acid Phenylalanine Tyrosine Tryptophan 5.66 5.48 9.59 5.89 Abbreviation/ symbol 6.14 Phe F Tyr Y Trp W pk, M, (-COOH) 165 181 204 . 1.83 2.20 2.38 Using the table 3-1, calculate the pl of Tyrosine. Hint: Consider the structure and overall charge of the molecule between each pka. pK₂2 (-NH) 9.13 9.11 9.39 PKR (R group) 10.07The octapeptide gly-cys-met-asn-lys-ala-tyr-gly was hydrolyzed consecutively by CNBr and then trypsin (3 fragments total). The mixture of fragments was buffered at a pH 8.5 and then chromatographed on an anion-exchanger (positive resin) with the same buffer. Draw sequence (abbreviated form) of all fragments at that pH (show charges) and predict elution order.