Be sure to answer all parts.Give the amino acid sequence of an octapeptide that contains the amino acids Val, Met, Asp (2 equiv),Phe, Trp, Ile, Lys, and forms the following fragments when partially hydrolyzed with HCl:Ile-Asp-Phe, Lys-Met-Val-Trp, andPhe-Asp-Lys-Met.TrpLeuPheLeuValLysGlyTyrX

Proteins are composed of amino acids. They are linked together by peptide linkages. Proteins have…

Answered: Be sure to answer all parts. Give the…

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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Be sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Thr, Phe, Ile (2 equiv), Asp, Cys, Val, Leu, and forms the following fragments when partially hydrolyzed with HCl: Thr-Ile-Phe, Phe-Ile-Asp-Val, and Asp-Val-Cys-Leu.
PRACTICE NAMING. Identify the number of amino acids, number of peptide bonds, and name the peptide. i.e. Ala-Cys • Dipeptide • 1 peptide bond • Alanylcysteine Cys-tyr-phe-gln-asn-cys-pro-arg-gly
Be sure to answer all parts. Draw the s-trans and s-cis conformations of the peptide bond in the dipeptide Ala-Ala. Be sure to show appropriate stereochemistry for the natural amino acid and the alkenes. I I I I I draw structure... s-trans draw structure ... s-cis
Pro-Ser-Ala-Phe-Glu. Draw this peptide at pH 7 and include its stereochemistry.
NOTE: PLEASE SEND. CLEARER IMAGE PLEASE THANK YOU SOMUCH 2. Structural representation of tetrapeptide Phe-Met-Tyr-Asn
. A nervous polecat. Pyrrolysine (Pyl, O) and Selenocysteine (Sec, U) are two uncommon amino acids. Knowing that these amino acids exists, translate the following amino acid sequence into one – letter code: Thr – Trp – Ile – Thr – Cys – His – Tyr – Leu – Ile – Thr – Thr – Ile – Glu – Phe – Glu – Arg – Arg – Glu – Thr – Ala – Arg – Glu – Asn – Thr – Tyr – Pyl – Sec – Met – Ala – Leu – Phe – Pyl – Tyr.
V-A. Which of the following amino acids will elute first in a cation-exchange column using a buffer at pH 7? 1. Asp or Lys 2. Arg or Met 3. Gly or Val 4. Ser or Ala
Do not give handwriting solution. Draw A mixed triacylglycerol that contains one saturated 8 - carbon fatty acid chain and two 6 - carbonfatty acid chains with 2 trans double bonds each.
Correlation between lipid profile and Covid-19.Explain this statement.
. Separating Glycated Hb From Normal Hb (Integrates with Chapters 5and 6.) Human hemoglobin can react with sugars in the blood(usually glucose) to form covalent adducts. The a-amino groups ofN-terminal valine in the Hb b-subunits react with the C-1 (aldehyde)carbons of monosaccharides to form aldimine adducts, whichrearrange to form very stable ketoamine products. Quantitation ofthis “glycated hemoglobin” is important clinically, especially fordiabetic individuals. Suggest at least three methods by which glycatedHb (also referred to as HbA1c) could be separated from normal Hband quantitated
Peptides. 1. Draw the peptide Ala-Glu-Gly-Lys, as it would occur at physiological pH = 7.4. The R groups of Ala and Gly are not acidic or basic, therefore do not have a pka and the charge on these R groups is therefore independent of pH. Glu is acidic and Lys is basic, therefore the charge on these amino acids is pH dependent. The pKas are shown below. pKa N-term = 9.0 C-term = 3.5 Glu4.1 Lys = 10.5 2. Draw a circle around the peptide bonds. 3. Label the C-terminus and the N-terminus. 4. What is the overall charge on the peptide at pH 7.4?
No plagiarism please. Use your own words. Thanks. Discuss the preferred locations of different classes of amino acids in transmembrane proteins. Explain the formation of thioether-linked prenyl anchor proteins. Explain the structure of caveolae.

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