For the structure of lysine, which enantiomer is shown? Give correct detailed Solution with explanation needed with structure. don't give Handwritten answer A OH H NH2 H₂N a-Lysine B B-Lysine C D-Lysine D L-Lysine
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- A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)envellum.ecollege.com/course.html?courseld3D16522631&OpenVellumHMAC=85a7baea4e7d7b9e1c025b928e35fe16#10001 I Review Constants | Periodic Table The compounds commonly known as "amino acids" are actually a-aminocarboxylic acids. What carbonyl compounds should be used to synthesize the two amino acids shown here using reductive amination? Part A CH3CH NH2 Draw the molecule on the canvas by choosing buttons from the Tools (for bonds), Atoms, and Advanced Template toolbars. The single bond is active by default. +) H 120 EXP. . i CONT. L. CWhich Compound Is Oxidized To Benzoic Acid With K2Cr2O7 In Acidic Medium?
- Protein: SHAYNERSE Predict the products of the following reactions with the protein given, if there is none, write NO RXN. - Biuret reagent - KOH/Pb(CH2COO)2 - Glyoxilic Acid/Conc. H2SO - Hg/HNO3 - HNO3iso-butylchloride with CH3COONaThe dynorphins are a group of opioid peptides that play an importantrole in changes in the brain associated with cocaine addiction. One ofthese peptides, dynorphin A, contains the following amino acidsequence: Tyr–Gly–Gly–Phe–Leu–Arg–Arg–Ile–Arg–Pro–Lys–Leu–Lys.Draw the amino acids and peptide fragments formed when dynorphin A is treated with each reagent or enzyme: (a) chymotrypsin; (b) trypsin; (c)carboxypeptidase; (d) C6H5N=C=S.
- Please provide answers to both questions.Describe how the following function as drugs: (a) AZT (b) cisplatin (c) daunomycinThere are 20 common, naturally occurring amino acids from which all proteins are derived (as will be discussed in Chapter 25), although many other less common amino acids have been isolated from natural sources. Valine is one of the 20 common amino acids, and it was used as a starting material in the laboratory synthesis of an uncommon amino acid (Tetrahedron 1997, 53, 1151-1156). During one of the steps in the synthesis, compound 1 was treated with HBr under conditions that favor radical addition, giving stereoisomers 2 and 3. Draw the structures of 2 and 3, and describe their stereoisomeric relationship. H. LOCH3 HBr 2 + 3 hv H (S)-valine Modify the given copies of compound 1 to drawthe structures of 2 and 3. You can use the single bond tool to add/remove double bonds. CH2 CH2 H,C- H3C- -CH, -CH, Edit Drawing Describe the relationship of 2 and 3. O They are enantiomers. O They are superimposable. They are diastereomers. O They are constitutional isomers.
- 2. Compound A, C;H100 , is one of the basic building blocks of nature. All steroids and many other naturally occuring compounds are built from compound A. Spectroscopic analysis of A yields the following information: IR: 3400 cm-'; 1640 cım- IH NMR: 1.63 & (3 H, singlet); 1.70 ô (3 H, singlet); 3.83 6 (1 H, broad singlet); 4.15 8 (2 H, doublet, j = 7 Hz); 5.70 ô (1 H, triplet, ) = 7 Hz) (a) How many double bonds and/or rings does A have? (b) From the IR spectrum, what is the identity of the oxygen-containing functional group? (c) What kinds of protons are responsible for the NMR absorptions listed ? (d) Propose a structure for A.This is a homework question... In nature, amino acids in proteins are typically found in the L-configuration. This is basedon it’s relationship to D- and L-glyceraldehyde. Shown below is the structure of the amino acidasparagine (Asn) at physiological pH. As written does histidine have an L(S)- or D(R)-configuration? Be sure to show how you derived your answer:Draw a pentapeptide, peptide sequence: IENAP Show the position of all 'heavy' atoms with the appropriate letter (C, N, O, S etc.) and indicate the number of attached hydrogen atoms (no skeletal structures allowed).- Show the chirality of the alpha carbon of every residue as the L isomer (not required for Glycine). All trigonal planar groups must be shown explicitly with appropriate geometry. • Show all double bonds and/or partial double bonds. • Draw all ionisable groups as their most highly populated state at pH 7.4 Make the peptide bond between the fourth residue and proline the cis isomer.- Show all other peptide bonds as trans.e