4. What is the product of the following reaction.H2N -CH-CH-CH-C--HO-CH2CH2CH21) Ph--N=c=SIH,CH22) CF,CO,HCH2NHNHHN=NH2nido sbivloe o combjex15. What would be the product of the following reactions?TrypsinAla-Phe-Lys-Pro-Met-Tyr-Gly-Arg-Ser-Trp-Leu-HisChymotrypsinAla-Phe-Lys-Pro-Met-Tyr-Gly-Arg-Ser-Trp-Leu-His

Introduction Trypsin cleaves the peptide bonds at the C-side of Arg and Lys whereas Chymotrypsin…

14. What is the product of the following reaction. H2N -CH- -ÇH- CH-C- OH CH2 CH2 CH2 1) Ph-N=C=SIH, CH2 2) CF,CO,H CH2 NH NH C= ENH NH2 क bojungs c bolles 15. What would be the product of the following reactions? Trypsin Ala-Phe-Lys-Pro-Met-Tyr-Gly-Arg-Ser-Trp-Leu-His Chymotrypsin Ala-Phe-Lys-Pro-Met-Tyr-Gly-Arg-Ser-Trp-Leu-His

14. What is the product of the following reaction. H2N -CH- -ÇH- CH-C- OH CH2 CH2 CH2 1) Ph-N=C=SIH, CH2 2) CF,CO,H CH2 NH NH C= ENH NH2 क bojungs c bolles 15. What would be the product of the following reactions? Trypsin Ala-Phe-Lys-Pro-Met-Tyr-Gly-Arg-Ser-Trp-Leu-His Chymotrypsin Ala-Phe-Lys-Pro-Met-Tyr-Gly-Arg-Ser-Trp-Leu-His

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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1. Amino acid analysis of the peptide gave the following residues: Asp Leu Lys Met Phe Tyr. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was C-C-CH2. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys. What is the amino acid sequence for this heptapeptide?
1. Label the ALPHA-Carbon, AMINO Group, CARBOXYL Group, and AMINO Side Chain of the following amino acids:- Proline- Glycine- Aspartic acid- Asparagine- Lysine 2. Write the structure of the following polypeptide chainsa.) Asp-Leu-Serb.) Thr-Trpc.) Gln-Ala-Prod.) Ile-Met-Cys-Glu
Rank these amino acids from most to least hydrophobic. H #3 13N-C-H CH₂OH 1 Q .000 OB) 3>2 > 1 E D A) 1>3>2 C) 3 >1 > 2 $ 4 R F % 5 coo™ H₂N-C-H T + __8_5 A CH 2 CH₂ CH₂ 3 2 6 CH MacBook Pro Y & 7 G | H U * 00 8 J 1 + _000 H₂N-C-H CH ₂ 1 CH₂ _000 9 3 K O 0 L d
Certain enzymes catalyze the covalent linkage of an acetyl group to lysine amino acids as shown below. When a particular target protein is in the un-acetylated state, its interacting partner protein will not bind. However, once acetylated, the partner protein can bind to this target protein. Which of the following can you conclude? Select all that apply CH CO NH 3. NH Lysine acetylation reaction CH, CH, +HaN -C- CO- H. HIN-C- Co- H. UAcetylation changes the secondary structure of the target protein The partner protein has acidic residues in the interacting region Acetylation changes the tertiary structure of the target protein The partner protein has basic residues in the interacting region 8-1-8-8-8–8–d=
The primary structure of b-endorphin, a peptide containing 31 amino acids synthesized by the body to control pain, is shown here: Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr- Leu-Phe-Lys-Asn-Ala-Ile-Ile-Lys-Asn-Ala-Tyr-Lys-Lys-Gly-Glu What fragments are obtained as a result of treatment with trypsin?
Place each charge form of alanine under the pH condition where it would be the predominant form. The pK₁ values for the carboxyl group and amino group of alanine are approximately 2.3 and 9.7, respectively. pH 11 H | H₂C-C-COO NH₂ Does not occur in significant amounts at any pH
The reverse synthesis of ceramides synthesized biologically from sphingosine is possible. 1. What type of reaction would this be? 2. How would the pH of the skin where this reaction is most likely to take place affect this reaction?
6. Which class or reactions results in the degradation of all macromolecules: a) dehydration synthesis of monomersà polymers with the loss of an H2O with the addition of each monomer b) hydrolysis with the addition of one H2O for each reaction c) oxidation with the loss of an e- d) reduction with the gain of an e-
Please answer the following questions 1) based on the structures of adenine, cytosine, guanine, and thyme. Why does A prefer to bind to T and C prefer to bind to G 2) were the binding energies the same for AT and CG? Explain the difference 3) which of the four know bases is the unknown synthetic base most like in terms of its binding characteristics? What does this indicate about its structure? 4) if the unknown synthetic base was used to study DNA replication, which natural bases would it interact with? 5) is the picture question
13. The structures of sphingosine and choline are given below. Draw the condensed structure and block diagram of the sphingolipid formed from these molecules and a molecule of myristic acid. CH3-(CH2)12-CH=CH-CH-OH CH₂ CH3-N-CH2-CH2-OH CH-NH2 sphingosine CH2-OH CH3 choline BLOCK DIAGRAM (draw below) CONDENSED STRUCTURE 14. Which fatty acid below should have the highest melting point? Why? Explain your answer based on structure and forces of attraction. OH O OH TOH OH
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draw all the structures of the tribasic amino acid lysine involved in the equilibrium reactions that would take place during titration against NaOH, starting with the fully protonated form below (draw the R-group in full). H;N+- CH - COOH (CH2)4 NH3+