E. PROTEIN PRIMARY STRUCTURE ELUCIDATION. 1. Determine the primary structure of the protein described below. Write the final sequence using the corresponding three-letter code for each amino acid. Example: M-F-Y-R should be written as Met-Phe-Tyr-Arg Treatment with cyanogen bromide and sequencing yields the following peptide fragments: D-M o R-A-Y-G-N o L-F-M • Chymotrypsin digestion and sequencing yields the following peptide fragments: o G-N o D-M-L-F o M-R-A-Y

E. PROTEIN PRIMARY STRUCTURE ELUCIDATION. 1. Determine the primary structure of the protein described below. Write the final sequence using the corresponding three-letter code for each amino acid. Example: M-F-Y-R should be written as Met-Phe-Tyr-Arg Treatment with cyanogen bromide and sequencing yields the following peptide fragments: D-M o R-A-Y-G-N o L-F-M • Chymotrypsin digestion and sequencing yields the following peptide fragments: o G-N o D-M-L-F o M-R-A-Y

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter3: Biological Macromolecules

Section: Chapter Questions

Problem 23CTQ: Amino acids have the generic structure seen below, where R represents different carbon-based side...

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Amino acids have the generic structure seen below, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.
The peptide below -NH-CH- H3N-CH- CH3 NH-CH- -NH-CH- -O- -NH-ÇH- CH2 CH2 CH2 HN-ç=NH, NH2 CH2 CH2 CH Ho-CH, C-OH H,C CH3 needs to be separated from a second peptide with a primary sequence ADES. At what pH range would it be possible to separate the peptides? O 0- 2.0 O 2.5 - 3.5 O 4.0 - 9.0 O 13.0 -14.0 о 10.0-12.0
Chymotrypsin digestion, separation of peptides, and Edmann technique give the sequences for peptide fragments as follows: C-1 G-A-E-A-T-E C-2 G-K-V-G-A-H-A-G-E-Y C-3 V-L-S-P-A-K-T-N-V-K-A-A-W What is the sequence for the peptide? NOTE: Label the fragments when reconstructing the peptide chain e.g. for trypsin T-1, T-2 etc...
Determining the amino acid sequence in a protein usually in- volves treating the protein with various reagents that break up the protein into smaller fragments that can be individually sequenced. Treating a particular 11-amino acid polypeptide with one reagent produced the fragments: Ala-Leu-Phe-Gly-Asn-Lys Trp-Glu-Cys Gly-Arg Treating the same polypeptide with a different reagent pro- duced the fragments: Glu-Cys Gly-Asn-Lys-Trp Gly-Arg-Ala-Leu-Phe What is the amino acid sequence of the polypeptide?
27. Draw palmitic acid, identify a, B and w carbons, write out its short hand notation 28. Examine the peptide sequence below and then answer the questions: H2N-Gly- Leu- Ala-Asp-Cys-Asn-Trp-lle-Ser-Phe-Lys-Cys-Arg-Pro-coOH a. Circle the asparagine residue b. A possible intramolecular disulfide bond can be formed within this peptide between which two residues? c. Circle one residue which has a positively charged side chain under pH 7.4 d. Circle one residue which has a negatively charged side chain under pH 7.4 e. Circle the residue which can be phosphorylated
Identify the sequence'of the peptide below. C-N-CH-COOH C-N-CH- H H CH- H,N*-CH-Ċ-N-CH-Ċ-N-CH-Ö-N-CH-Ċ- H CH, CH2 ČOOH H CH, H CH, H CH, CH, CH, CH2 *NH, H CH, он CH, SH S CH, O CAEKGSM O MSGKEAC O CAKEGMS O KEACMSG
B. Enumerate all the possible DNA nucleotide base sequence for the amino acids given. 4. Met – Leu – Ala - Gly- Glu - Gly- Gln- Glu- Ala - Ala - Pro - Leu
Topic: ISOLATION AND CHARACTERIZATION OF PROTEINS 1. Which amino acids contains the following:a. Sulfur/sulfhydryl groupb. Aromatic groupc. Imidazole ringd. Guanidine groupe. Indole ring2. Classify the following proteins to their biological functions (casein, albumin, gluten, andmyoglobin) 3. Which level of protein structure organization are lost hydrolysis and denaturation?4. What is the Beer-Lambert’s Law? Why is it relevant to the quantitative analysis of proteins?
The sequence of a 29 aa long peptide can be determined from the following data: Treatment of the peptide with dansyl chloride reveals that the amino-terminal is Val. Trypsin digestion, separation of peptides, and Edmann technique give the sequences for peptide fragments as follows: T-1 V-G-A-H-A-G-E-Y-G-A-E-A-T-E T-2 A-A-W-G-KT-3 V-L-S-P-A-K T-4 T-N-V-K
困 STRUCTURE AND NOMENCLATURE Name the fourth nucleotide from the 3' to 5' end. Use the How many terminal phosphate/s is/are present in the given structure? Give correct/appropriate punctuations, spacing and letter case based on the nomenclature. ONLY the NUMBER of the terminal phosphate/s. NH, O P-0 OP-O- OH 0=-0- NH: NH: NH; NH. 0=P-0- OH 0P-0- 0P-0- 0=P-0- OH 9:53 am P Type here to search 4) ENG 13/10/2021 近

a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain
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. /