ẞ-Calendic acid is an omega-6, conjugated fatty acid that is the all-trans isomer of a-calendic acid.HOOC—CH,CH, CH, CH,CH, CH,Part: 0/2Part 1 of 2HC=CHC-HH-CHC=CHCH₂-CH2-CH2-CH2-CH₂When this fatty acid is partially hydrogenated with one equivalent of H₂ in the presence of a Pd catalyst, a mixture of constitutional isomers is formed.Modify the given structure to draw one of these possible products.

Polyunsaturated fatty acids (PUFA) are fatty acids with more than one double bond. Complete…

Answered: ẞ-Calendic acid is an omega-6,…

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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Similar questions

The OH group of the serine side chain (R-OH) can undergo dissociation to form R-O- and H+. However, the ratio of the protonated to unprotonated forms of this group at pH 7 is approximately 1,000,000 to 1. Calculate the pKa of the serine OH group.
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
A hemoglobin molecule is made up of four polypeptide chains, two alpha chains of 141 amino acid residues each and two beta chains of 146 amino acid residues each. In the complete molecule, four subunits are closely joined, as in a three-dimensional jigsaw puzzle, to form a tetramer. Hemoglobin is showing level of structure O primary secondary tertiary quarternary O pentameric
The amino acid residue sequence of the hemoglobin beta subunit polypeptide would represent what type of structure? O PRIMARY O SECONDARY O TERTIARY O QUATERNARY
After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?
Draw the zwitterion for each of the following amino acids: glycine threonine glutamic acid phenylalanine
Copy of The following reaction scheme shows the states of the amino acid hisitdine. Histidine has three pKa's - 2, 6 and 9.2. Which form of Histidine predominates at pH of 5? *H3N-CH-Ĉ-OH CH2 *H3N-CH-C–O- CH2 "H3N-CH-C-O- CH2 H2N-CH-C–O- CH2 +HN *HN N' -NH -NH -NH NH A C O A. A ОВ. В OC.C O D.D O E. The answer cannot be determined with information given.
Write the one letter code for the oligopeptide Ser-Cys-Ile-Glu-Asn-Cys-Glu and calculate the total charge on it at pH 4.5.
Draw the structures of the products formed by hydrolysis of the following tripeptide at physiological pH. Val-Gly-Ile Note: Reference the Naturally occurring amino acids data table for additional information.
Give the amino acid sequence of an octapeptide that contains the amino acids Tyr, Ala, Leu (2 equiv), Cys, Gly, Glu, and Val, and forms the following fragments when partially hydrolyzed with HCI: Val-Cys-Gly-Glu, Ala-Leu-Tyr, and Tyr-Leu-Val-Cys.
An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.
Consider the following two peptides: I. N-Pro-Pro - Glu - Glu - Tyr - His - Cys - Ala - Glu - Gln - Lys - Leu - Ser - Ser - Phe-Leu- Thr - C II. N-Pro-Pro - Lys - Arg - Gly - Tyr - His - Gly - Glu - Asp - Glu - Asp - Glu - Ser - Gly-Phe- Tyr-C Give three reasons why_peptide I is more likely to form an alpha helix in aqueous solution at pH 7.0. Your reasons may include why_peptide Il is less likely to form an alpha helix

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