A protein has a number of aspartyl and gluatmyl residues, what would be the expected pl for this protein?a.b.O C.O d.Neutral plAcidic plCannot be determined.Basic pl Consider the hydrogen bonding pattern of an a-helix with the following sequence:Asparagine's carbonyl oxygen is hydrogen bonded to:Lysine's backbone amide hydrogenO aOb Aspartate's backbone carbonyl oxygenOc. Tyrosine's backbone amide hydrogenSerine's backbone amide hydrogenOdLeucine's side chainOe.DLRANGCTSY

pI refers to the isoelectric point of a molecule, including proteins. It is the pH at which the…

Answered: A protein has a number of aspartyl and…

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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Give explanation of all four otherwise leave it
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A protein has an asp glu/arg lys ratio of 3. What would the overall charge on this molecule likely be at pH 7? positive negative none of the above
10. A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the physiological protein has a molecular weight of 240,000 Daltons. Chromatography in the presence of 6 M urea yields a single peak corresponding to a protein of 60,000 Daltons. Chromatography in the presence of 6 M urea and 10 mM mercaptoethanol yields peaks for proteins of 34,000 Daltons and 26,000 Daltons. What can we learn about protein's tertiary and quaternary structure from this data?
4. Deducing quaternary structure via SDS-PAGE. SDS-PAGE is a convenient method for separating polypeptides solely on the basis of size. Small polypeptides travel faster than large ones; rate of migration through the gel is inversely proportional to the logarithm of molecular weight. The subunit structure of a multimeric protein often can be deduced using this technique in conjunction with a protein cross-linking agent. Cross-linking agents react with amino acid residues of two polypeptides that are in contact, thereby linking them by covalent bonds. After limited treatment with the reagent, so that some but not all subunits become cross-linked to their neighbors, the protein is subjected to SDS-PAGE and the molecular weights of the resulting proteins (bands) are estimated. The results of such experiments on two proteins (Protein A and Protein B) are shown below. What is the most likely subunit structure of each protein? Protein A SDS-PAGE cross-linking agent MW 105,000 70,000 35,000…
provide detailed explanation.
Which type of amino acid would be found on the outside of a portion of a protein embedded in the membrane (up close to the fatty acid tails)? Select one: O a. a special amino acid like glycine or proline O b. a polar amino acid like serine Ос. a hydrophobic amino acid like valine Od. a charged amino acid like lysine O e. any of the above, with no preference Clear my choice Next page ure.pptx MacBook Pro
Which statement is NOT true about the figure below? O Major and minor grooves are shown here. Diameter is 2nm O Tertiary structure of a protein molecule is shown here. O The purple interior represents nitrogenous base pairs
Select the properties that apply to the secondary structure alpha helices (select all that apply). U 0 can be Antiparallel can be Parallel are typically right handed are typically left handed obeys n+4 rule are formed by the pattern of hydrogen bonding the backbone makes with itself are formed by the pattern of covalent bonds the backbone makes with itself are formed by the pattern of electrostatic attractions the backbone makes with itself
1. The hydropathic index represents the sum of hydrophobic and hydrophilic residues of a polypeptide. A.true B.false

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A protein has a number of aspartyl and gluatmyl residues, what would be the expected pl for this protein? 4 a O b. OC. Od Neutral pl Acidic pl Cannot be determined. Basic pl