In this problem consider how Glycine's charge changes with pH. You can find the pKas for the alpha-carboxylic and alpha-amino groups above. Determine the net charge at the following pH values. Theanswer options are rounded to the nearest 0.5 unit; please match each pH to the best choice.pH = 1pH = 2.35pH = 6pH = 9.78pH = 13+10-1.0-2.0-2.0

Glycine is the smallest of the twenty amino acids found in proteins. It has a simple structure with…

Answered: In this problem consider how Glycine's…

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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1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
The amino acid glycine is often used as an ingredient in buffers for biochemistry experiments. The amino group of glycine has a pKa of 9.6. Glycine exists in either a protonated form (-NH3+) or a free base (-NH₂). a) In what pH range can glycine be used as an effective buffer? b) In a 0.1M solution of glycine at pH 9.0, what fraction has its amino group in the protonated form? c) When 99% of the glycine is in the protonated from, what is the numerical relation between the pH of the solution and the pKa of the amino group?
Assume a pH of 7.0 in aqueous solution. Please draw a tripeptide containing (in this order) a residue with a residue with an non-polar sidechain containing more than five carbons, a positively (+1) charged sidechain, and a residue with a polar (but not charged) sidechain with more than two carbons. Please give the names of the amino acid residues that you drew.
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Please draw titration curves for peptide HFDTYA and HEKDGQ, and calculate the pl for each. Usethis information to explain why the peptide HFDTYA has low solubility and HEKDGQ has a highersolubility in bulk water at pH = 7.
Glutamic acid (1one of the 20 amino acids) has a side- chain carboxyl group (COOH, pKa = 4.3) as shown in Figures 4.7 and 4.8 a. Write the chemical equation for the dissociation of the side chain COOH. Label the weak acid and the conjugate base. b. The Henderson-Hasselbalch Equation (shown below) can be used to determine the ionization status of a weak acid: pH = pKa + log [base] Use the Henderson Hasselbalch equation to determine whether the glutamic acid side chain [acid] • carboxyl group is protonated or deprotonated at physiological pH.
The peptide aspartyl-glutamyl-leucyl-threonyl-alanine, shown in the sketch drawing window, has several ionizable groups. Adjust the charges to show the molecule as it would exist at pH 5.00. Use the pk values in the table below. pK, Values for Ionizable Groups of Amino Acids. Amino Acid pA, of a-COOH pA, of e-NH, pA, of Side Chain Isoelectric Point (pI) Alanine 235 9.87 6.11 Arginine 2.01 9.04 12.48 10.76 Asparagine 2.02 8.80 5.41 Aspartic acid 210 9.82 3.86 298 Cysteine 2.05 10.25 8.00 5.02 Glutzmic acid 2.10 9.47 4.07 3.08 Glutamine 217 9.13 5.65 Glycine 235 9.78 6.06 Histidine 7.11 9.18 6.10 7.64 Isoleucine 232 9.76 6.04 Leucine 233 9.74 6.04 Lysine 218 8.95 10.53 9.74 Methionine 2 28 9.21 5.74 Phenylalanine 2 58 9.24 5.91 Proline 2.00 10.60 6.30 Serine 221 9.15 5.68 Threonine 2.09 9.10 5.60 Trуptophan 238 9.39 5.88 Tyrosine 2 20 9.11 10.07 5.63 Valine 2 29 9.72 6.00 • Use the wedge hash bond tools to indicate stereochemistry where it exists. • If a group is 2chiral, do not use…
A purified protein fraction has a total sample volume of 360 µL. The sample has a corrected A280 of 0.484, and the blank corrected A280 was 0.052. (Both values were measured with a path length of 1.00 cm.) If 5.00 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).

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