SavedQuestion 264At pH 12.48, arginine (pK's 1.82, 8.99, 12.48) would be charged as follows:O 1) -1 alpha-carboxyl, 0 alpha-amino, +0.5 guanidino, -0.5 net chargeO 2) 0 alpha-carboxyl, 0 alpha-amino, +1 guanidino, +1 net charge3) +1 alpha-carboxyl, -1 alpha-amino, -1 guanidino, -1 net chargeO4) +1 alpha-carboxyl, 0 alpha-amino, -1 guanidino, O net charge5) 1 alpha-carboxylate, +1 alpha-amino, +1 guanidino, +1 net charge

The pKa of the ionizable groups of an amino acid is important for determining the net charge on the…

Answered: At pH 12.48, arginine (pK's 1.82, 8.99,…

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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The pH vs charge graph for a triprotic amino acid is shown below. Please answer the following questions about the amino acid. Net Charge 0 2 4 Alpha amino [Select] 6 R [Select] pH a. Which of the following triprotic amino acids is this? Alpha carboxyl [Select] 8 10 12 [ Select] 14 1 0.5 0 -0.5 -1 b. What is the isoelectric point? (Please select the appropriate range in which the isoelectric point falls) (Hint - look up the pKa values in the pKa table for amino acids, which was in video one of today's lecture) [Select] -1.5 c. What form of this amino acid dominates at a pH of 14? Please select the correct form for each ionizable group. -2
Stereochemistry in biological molecules is often denoted by the D- and L- convention, instead of the R- and S- configurations determined by the Cahn-Ingold-Prelog methodology. Naturally occurring α-amino acids are typically in the L-configuration. The Fischer projection of L-alanine is shown. L-alanine H₂N- H3C- HOOC Identify which structures are equivalent to the L-configuration. H COOH H CH3 NH₂ -COOH NH₂ CH3 -H CH3 COOH H -NH₂ H₂N- H CH3 COOH NH₂ H CH3 -COOH
The E. coli enzyme triose phosphate isomerase has a pI of 5.7. What would the charge on this enzyme be below a pH of 5.7? What about above? What would the charge be at a pH of 5.7?
What is the principal form of arginine at pH 8.0? Approximately what fraction is in this form?
Which of the twenty naturally occurring amino acid side chains are charged at a pan of 1.00? pH of 7.00? pH of 12.00? Make a table.
Titration of alanine by a strong base, for example NaOH, reveals two pk's. Which is the titration reaction occurring at pK1 (pK1 = %3D 2.34)? O-NH2 + COH →-NH + H2O O-COOH + OH →-CO + H20 -COOH + -NH2 → -COO" + -NH2+ -CoO +-NH2* → -COOH +-NH2 O -NH3* + OH →-NH2 + H2O
A) Refer to the figure below, Identify and explain the two types of reactions, and describe what are the importance of these reactions to our bodies. Reaction 1 H Monomer Reaction 2 H H OH + H H H₂O H H₂O OH + H H OH OH + H H₂O H₂O OH OH + H OH OH OH OH B) What are the main chemical interactions that determine and maintain the quaternary structure of proteins. Also, what are the conditions that can alter these interactions? [
This amino acid is: (Note that the non-ionized form is shown; remember that backbone groups are irrelevant to classification) a) Polarized (+) charged b) Nonpolar c) Polar and (-) charged d) Polar uncharged
Φ and ψ in the Ramachandran plot (below) are: a) Rotational angles around the bond between the α-carbon and N-H (Φ) and C=O (ψ). b) Amino acid solubility in octanol (Φ) and water (ψ). c) Hydrogen bond angles in α-helices (Φ) and β-sheets (ψ). d) Amino acid solubility in water (Φ) and octanol (ψ).
The carbon-nitrogen peptide bond is rigid, but rotation can take place about the N-Ca and the Ca-C bonds in a protein (Ca is the a carbon atom). These bond angles define the conformation of the peptide chain. Consider the Ramachandran plot to answer both questions. Which dihedral angles and residues would not likely occur in a ß sheet? 180 120 60 -60 -120 -180 -180 180 + (degrees) OA. 0=-51°; U=+153°; many Gly and Pro residues D=+60°; u=+60°; many Gly residues В. OC. D=-57°; W=-49°; many Ala residues D=-139°; W=+135°; many Val residues OD. D=-120°; U=+120°; many Tyr residues DE. (səəbap)
The pka of the side chain of histidine is 6.00. What is the percent of protonated histidine at pH 6.4? 15.3% 28.5% 45.3% O 66.6%
Compare the stability of the two salt bridges shown circled in blue at pH 8.4. The carboxylate ions are completely de- protonated at pH 8.4 The pka of the amino group (upper left) is 8.1 and the pka of the amino group (bottom right) is 8.7. (d) NH, F-8- Ed (b) O-H- M5 CH₂COOH (c) 5 (b) CH, CH. H--O=C (d) -H H CH,OH (b) KCHJ NH, (a) The bottom right salt bridge is stronger due to the partial positive charge of +2/3. The bottom right salt bridge is stronger due to the partial positive charge of +1/3. The upper left salt bridge is stronger due to the partial positive charge of +1/3. The upper left salt bridge is stronger due to the partial positive charge of +2/3.

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