Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 2, Problem 3P
Interpretation Introduction
Interpretation:
The given amino acids should be matched to the appropriate given side chain type.
Concept introduction:
Amino acids are so named because they all are weak acids. All amino acids have at least two dissociable hydrogens, (diprotic), and some have three dissociable hydrogens and are triprotic.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Draw the predominant form of
glutamic acid at pH = 8.4. The pKa
of the side chain is 4.1. Include
proper stereochemistry.
HO
H2N
OH
pH = 8.4
How would I draw this?
Calculate the standard change in Gibbs free energy, AGrxn, for the given reaction at 25.0 °C. Consult the table of
thermodynamic properties for standard Gibbs free energy of formation values.
NH,Cl(s) →NH; (aq) + C1 (aq)
AGrxn
-7.67
Correct Answer
Determine the concentration of NH+ (aq) if the change in Gibbs free energy, AGrxn, for the reaction is -9.27 kJ/mol.
6.49
[NH+]
Incorrect Answer
kJ/mol
M
Chapter 2 Solutions
Biochemistry
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- What are some topics of interest that neurotoxicologists study? For example, toxin-induced seizures, brain death, and such along those lines?arrow_forwardCould you help me with the explanation of the answer to exercise 15, chapter 1 of Lehinger Question Nombramiento de estereoisómeros con dos carbonos quirales utilizando el sistema RS(R,R)El isómero del metilfenidato (Ritalin) se utiliza para tratar el trastorno por déficit de atención con hiperactividad (TDAH).(S,S)El isómero es un antidepresivo. Identifique los dos carbonos quirales en la siguiente estructura. ¿Es este el(R,R)o el(S,S)¿isómero? Dibuja el otro isómero. Nombramiento de estereoisómeros con dos carbonos quirales utilizando el sistema RS(R,R)El isómero del metilfenidato (Ritalin) se utiliza para tratar el trastorno por déficit de atención con hiperactividad (TDAH).(S,S)El isómero es un antidepresivo.arrow_forwardThe reaction A+B → C + D AG°' = -7.3 kcal/mol can be coupled with which of the following unfavorable reactions to drive it forward? A. EFG+HAG° = 5.6 kcal/mol. B. J+KZ+A AG° = 2.3 kcal/mol. C. P+RY+DAG° = 8.2 kcal/mol. D. C + T → V + W AG°' = -5.9 kcal/mol. E. AN→ Q+KAG°' = 4.3 kcal/mol.arrow_forward
- What would be the toxicological endpoints for neurotoxicity?arrow_forwardWhat are "endpoints" in toxicology exactly? Please give an intuitive easy explanationarrow_forwardFura-2 Fluorescence (Arbitrary Unit) 4500 4000 3500 3000 2500 2000 1500 1000 500 [Ca2+]=2970nM, 25°C [Ca2+] 2970nM, 4°C [Ca2+]=0.9nM, 25°C [Ca2+] = 0.9nM, 4°C 0 260 280 300 340 360 380 400 420 440 Wavelength (nm) ← < The figure on the LHS shows the excitation spectra of Fura-2 (Em = 510 nm) in 2 solutions with two different Ca2+ ion concentration as indicated. Except for temperature, the setting for excitation & signal acquisition was identical.< ப a) The unit in Y-axis is arbitrary (unspecified). Why? < < b) Compare & contrast the excitation wavelength of the Isosbestic Point of Fura-2 at 25 °C & 4 °C. Give a possible reason for the discrepancy. < c) The fluorescence intensity at 25 °C & 4 °C are different. Explain why with the concept of electronic configuration. <arrow_forward
- draw in the structure of each amino acid (as L-amino acids) using the Fischer projection style. an example has been included. Draw the structure for glycine, alanine, valine, isoleucine, methionine, proline, phenylalanine, tryptophan, serine, threonine, asparagine, glutamine, lysine, arginine, aspartic acid, glutamic acid, histidine, tyrosine, cysteinearrow_forwarddraw in the structure of each amino acid (as L-amino acids) using the Fischer projection style. an example has been includedarrow_forwarddraw in the structure of each amino acid (as L-amino acids) using the Fischer projection style. an example has been includedarrow_forward
- Draw out the following peptide H-R-K-E-D at physiological pH (~7.4). Make sure toreference table 3.1 for pKa values.arrow_forwardThe table provides the standard reduction potential, E', for relevant half-cell reactions. Half-reaction E'° (V) Oxaloacetate² + 2H+ + 2e malate²- -0.166 Pyruvate + 2H+ + 2e → lactate -0.185 Acetaldehyde + 2H+ + 2e¯ →→→ ethanol -0.197 NAD+ + H+ + 2e--> NADH -0.320 NADP+ + H+ + 2e →→ NADPH Acetoacetate + 2H+ + 2e¯ - -0.324 B-hydroxybutyrate -0.346 Which of the reactions listed would proceed in the direction shown, under standard conditions, in the presence of the appropriate enzymes? Malate + NAD+ oxaloacetate + NADH + H+ Malate + pyruvate oxaloacetate + lactate Pyruvate + NADH + H+ lactate + NAD+ Pyruvate + p-hydroxybutyrate lactate + acetoacetate Acetaldehyde + succinate ethanol + fumerate Acetoacetate + NADH + H+ → B-hydroxybutyrate + NAD+arrow_forwardArrange the four structures in order from most reduced to most oxidized. Most reduced R-CH2-CH3 R-CH2-CH₂-OH R-CH,-CHO R-CH₂-COO Most oxidizedarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage Learning
Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Human Heredity: Principles and Issues (MindTap Co...BiologyISBN:9781305251052Author:Michael CummingsPublisher:Cengage Learning
Biology: The Unity and Diversity of Life (MindTap...BiologyISBN:9781337408332Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa StarrPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Biology (MindTap Course List)
Biology
ISBN:9781337392938
Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher:Cengage Learning
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Human Heredity: Principles and Issues (MindTap Co...
Biology
ISBN:9781305251052
Author:Michael Cummings
Publisher:Cengage Learning
Biology: The Unity and Diversity of Life (MindTap...
Biology
ISBN:9781337408332
Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr
Publisher:Cengage Learning
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY