01DescriptionPlease draw the structure of the 19 L-a-amino acids and proline inany form, as you prefer. You may want to use a letter-size sheet orlarger, it's up to you.Guiding principle: You want to understand the differences amongamino acids. Although you may want to only draw the R-group it'spreferable to draw it along with the rest of the molecule (i.e., theCa, the amino group and the carboxyl group).Here are some examples (your drawings should not limited to thefollowing styles):NH₂OHAlanineHHOOHProlinelysinealarmy stock płwłosTryptophanOHCOOH|H₂N-C-HCH₂Phenylalaninearginine

Amino acids are the monomer units that make up polypeptides, that eventually folds to become…

Answered: Please draw the structure of the 19…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Description Please draw the structure of the 19 L-a-amino acids and proline in any form, as you prefer. You may want to use a letter-size sheet or larger, it's up to you. Guiding principle: You want to understand the differences among amino acids. Although you may want to only draw the R-group it's preferable to draw it along with the rest of the molecule (i.e., the Ca, the amino group and the carboxyl group). Here are some examples (your drawings should not limited to the following styles): H₂C NH₂ OH shutterstock.com-222977980 Alanine H H Proline OH %%% lysine a alamy stock photo Tryptophan HN NH₂ shutterstock.com-1819000134 QH COOH H₂N-C- H CH ₂ Phenylalanine H₂N NH dreamstime.com arginine NH₂ OH
Draw peptide Pro-Ser-Ala-Phe-Glu as you would see it at pH 7. Include stereochemistry.
Draw the Ala-Ser-Leu-Asp polypeptide (perspective formula) showing the fully extended backbone geometry (all angles +/- 180°). Include correct stereochemistry for L-amino acids. Label all bond rotations representing the angles at each residue
0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.
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: o D-M o R-A-Y-G-N o L-F-M Chymotrypsin digestion and sequencing yields the following peptide fragments: o G-N D-M-L-F o M-R-A-Y o o
Asp-Gly-Lys-Glu-Ile-Phe Draw its full chemical structure as it would exist at pH = 7.0. Draw an arrow pointing to each peptide bond. Identify the net charge of the peptide and briefly explain how you arrived at this answer.
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
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?
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
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

N - Leucine - Arginine - Proline - Aspartic acid - Methionine - C write the structure classify the type of peptide number of peptide bonds IUPAC name 3 - and 1 letter abbrevation. Solve for pI Determine the charge @ pH = 1, 3, 5, 10 & 13
Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show them in zig-zag style, from amino to carboxy terminus, with correct stereochemistry Draw the predominant form at pH = 2 Draw the predominant form at pH = 5 Draw the predominant form at pH = 7 Draw the predominant form at pH = 12

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Please draw the structure of the 19 L-a-amino acids and proline in any form, as you prefer. You may want to use a letter-size sheet or larger, it's up to you.