Spell out the name of the polypeptide using three letter codes for each amino acid separated with hyphens (for example, Tyr-Lys-Trp).
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Q: Give the name of the polypeptide
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Q: Draw and label the following RNA tetranucleotide: 5'phosphoryl-A-2'O-methyl-C-U-G-3'- phosphate.
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Q: Write the anticodons for the following amino acids: a) Met b) Trp c) Ser d) Leu
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- Determine the sequence of the decapeptide given the following information below. The decapeptide was hydrolyzed and confirmed to contain these amino acids: E, F, K, M, Q, S, T x 3, W Edman degradation product of the decapeptide: T trypsin fragments: a tetrapeptide (F,K,Q,T) and a hexapeptide (E,M,S,2T,W) chymotrypsin fragments: free S, a dipeptide (F,T) and a heptapeptide (E,K,M,Q,T,T,W) CNBr treatment of the heptapeptide (E,K,M,Q,T,T,W) yielded a tetrapeptide (K,T,M,Q) and a tripeptide (E,T,W) Edman degradation product of (E,T,W): E Use one-letter abbreviations only. One amino acid per blank.PRECIPITATION OF PROTEINS What are peptides? Do all proteins possess peptide bonds? Do all proteins respond to Biuret’s test? What is the difference between coagulation and denaturation? Why is egg white used as an antidote for lead and mercurial poisoning? Explain its mechanism of action. 4.Why is silver nitrate used in the cauterization of wound? Explain your answer.TOPIC: Precipitation of Proteins by Heavy Metal Salts 1. In what way can ingestion of heavy metals, such as lead and mercury, be detrimental to the proteins in your body? ____________________________________________________________________ ____________________________________________________________________ 2. Why is egg white used as an antidote for lead and mercury poisoning? ____________________________________________________________________ ____________________________________________________________________
- 1. Analysis of a peptide antibiotic purified from a strain of Bacillus brevii resulted in the following significant information: - Complete hydrolysis of the peptide yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val - Molecular weight of the peptide was estimated to be aroung 1,200 Da - The peptide failed to undergo hydrolysis when treated with carboxypeptidase - Partial hydrolysis and then chromatographic separation of products yielded the following di- and tripeptides: Leu-Phe, Phe-Pro, Orn-Leu, Val-Orn, Val-Orn-Leu, Phe-Pro-Val, Pro-Val- - Orn Treament with dinitrofluorobenzene (DNFB) followed by complete hydrolysis yielded only free amino acids and the DNFB-derivatized ornithine at its side chain By using the above information, deduce the amino acid sequence of this peptide antibiotic. Write the final peptide sequence using 3-letter abbreviations. Show the complete and step by step solution.Modify isoleucine to show the predominant forms at pH 1, 7, and 13. Isoleucine has p?ap�a values of 2.4 (carboxyl group) and 9.7 (amino group).Check the TRUE alternative in relation to amino acids and proteins: (a) the precipitation of a protein is always an irreversible process (b) the isoelectric point of amino acids with non-ionizable side chain is reached at neutral pH (= 7) (c) all the amino acids that make up our proteins have a chiral carbon whose configuration is (S) (d) denaturation affects all structural levels of proteins (e) all amino acids are soluble in water and have relatively high melting points
- What is the dissociation equilibrium constant of a protein if the concentration of free ligand is 3.0um when the fraction of bound sites is 0.6Quantitative Estimation of Amino Acids by Ninhydrin http://vlab.amrita.edu/?sub=3&brch=63&sim=156&cnt=2 can u help me with question 2 of the assignment questions Based on the experimental data provided, estimate the amount of amino acid in the given unknown solution by Ninhydrin method. SI No. Volume of standard amino acid solution (ml) Amount of amino acid (µg) OD at 570nm 1 Blank 0 2 0.2 0.12 3 0.4 0.25 4 0.6 0.45 5 0.8 0.55 6 1.0 100 0.68 7 Unknown (0.5ml) 0.41A peptide has the sequence: Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly1. What would be the net charge of the molecule at pH a) 3, b) 8, and c) 11? (Use pKa values. Do not calculate the value per se, but instead estimate considering only fully protonated, or deprotonated states. Then estimate the pI for this peptide. Show full, clear and complete procedure
- 2. A group of peptides that influence nerve transmission in certain parts of the brain have been isolated from normal brain tissue. These peptides are known as opioids. Using the information below, determine the amino acid sequence of this particular opioid: ● Complete hydrolysis by HCl at 100° C followed by amino acid hydrolysis analysis indicated the presence of Gly, Leu, Phe, and Tyr, in a 2:1:1:1 ratio. ● Treatment of the peptide with FNDB followed by complete hydrolysis indicated the presence of 2,2-dinitrophenyl derivative of tyrosine. No free tyrosine could be found. ● Complete digestion of the peptide with chymotrypsin yielded free tyrosine and leucine, plus a tripeptide containing Phe and Gly in a 1:2 ratio. Instructions Make use of the table below to determine the sequence of the mystery protein:VII. Analysis of a peptide antibiotic purified from a strain of Bacillus brevii resulted in the following significant information: Complete hydrolysis of the peptide yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val Molecular weight of the peptide was estimated to be aroung 1,200 Da The peptide failed to undergo hydrolysis when treated with carboxypeptidase Partial hydrolysis and then chromatographic separation of products yielded the following di- and tripeptides: Leu-Phe, Phe-Pro, Orn-Leu, Val-Orn, Val-Orn-Leu, Phe-Pro-Val, Pro-Val-Orn Treament with dinitrofluorobenzene (DNFB) followed by complete hydrolysis yielded only free amino acids and the DNFB-derivatized ornithine at its side chain Using this set of information available to you, deduce the amino acid sequence of this peptide antibiotic. Write your final peptide sequence only using 3-letter abbreviations.At pH 7.0, in what order would the following three peptides (described by their amino acid composition) be eluted from a column filled with a cationexchange polymer?Peptide A: Ala 10%, Glu 5%, Ser 5%, Leu 10%, Arg 10%, His 5%, Ile 10%, Phe 5%, Tyr 5%, Lys 10%, Gly 10%, Pro 5%, and Trp 10%.Peptide B: Ala 5%, Val 5%, Gly 10%, Asp 5%, Leu 5%, Arg 5%, Ile 5%, Phe 5%, Tyr 5%, Lys 5%, Trp 5%, Ser 5%, Thr 5%, Glu 5%, Asn 5%, Pro 10%, Met 5%, and Cys 5%.Peptide C: Ala 10%, Glu 10%, Gly 5%, Leu 5%, Asp 10%, Arg 5%, Met 5%, Cys 5%, Tyr 5%, Phe 5%, His 5%, Val 5%, Pro 5%, Thr 5%, Ser 5%, Asn 5%, and Gln 5%
