General, Organic, & Biological Chemistry
3rd Edition
ISBN: 9780073511245
Author: Janice Gorzynski Smith Dr.
Publisher: McGraw-Hill Education
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 21.3, Problem 21.5P
Identify the amino acid shown with all uncharged atoms in the ball-and-stick model, and draw theneutral, positively charged, and negatively charged forms of the amino acid.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Net charge and isoelectric point of an amino acid with an ionizable side group.Consider the net charge and isoelectric point of an amino acid with ionizable side (R-) group.(a) Identify the acidic amino acid(s) capable of having a negatively charged carboxyl side group.(b) Identify the basic amino acid(s) capable of having a positively charged amino side group.(c) For an amino acid with a side (R-) chain that can ionize to a negative charge, derive a general expression in terms of measured pH and known pKa values of α-carboxyla-amino (pKca), α-amino(pKaa),and side group (pKRa), respectively, for the net charge of an amino acid Consider the net charge and isoelectric point of an amino acid with ionizable side (R-) group.(d) For an amino acid with a side (R-) chain that can ionize to a positive charge, derive a general expression in terms of measured pH and known pKa values ofα-carboxyl (pKca), α-amino (pKaa), and side group (pKRa), respectively, for the net charge of the amino acid.(e)…
What does the "alpha" indicate in "α-amino acid"?
That the -COOH group is below the plane of the ring.
That the amino group is the first group in the compound.
That the alpha-carbon has a -NH2 attached.
The the amino acid is the dominant form.
Identify the amino acid shown with all uncharged atoms in the ball-and-stick model, and draw the neutral, positively charged, and negatively charged forms of the amino acid.
Chapter 21 Solutions
General, Organic, & Biological Chemistry
Ch. 21.2 - In addition to the amino and carboxyl groups, what...Ch. 21.2 - Draw both enantiomers of each amino acid in...Ch. 21.2 - Prob. 21.3PCh. 21.3 - Draw the structure of the amino acid valine at...Ch. 21.3 - Identify the amino acid shown with all uncharged...Ch. 21.4 - Identify the N-terminal and C-terminal amino acid...Ch. 21.4 - Prob. 21.7PCh. 21.4 - Prob. 21.8PCh. 21.4 - Prob. 21.9PCh. 21.4 - Prob. 21.10P
Ch. 21.4 - Prob. 21.11PCh. 21.5 - Prob. 21.12PCh. 21.6 - Prob. 21.13PCh. 21.6 - Prob. 21.14PCh. 21.6 - Prob. 21.15PCh. 21.7 - Why is hemoglobin more water soluble than ...Ch. 21.8 - Prob. 21.17PCh. 21.8 - Prob. 21.18PCh. 21.9 - Prob. 21.19PCh. 21.9 - Prob. 21.20PCh. 21.9 - Prob. 21.21PCh. 21.9 - Prob. 21.22PCh. 21.10 - Prob. 21.23PCh. 21.10 - Prob. 21.24PCh. 21.10 - Prob. 21.25PCh. 21.10 - Prob. 21.26PCh. 21.10 - Prob. 21.27PCh. 21.10 - Prob. 21.28PCh. 21.10 - Prob. 21.29PCh. 21.11 - Prob. 21.30PCh. 21 - The amino acid alanine is a solid at room...Ch. 21 - Why is phenylalanine water soluble but...Ch. 21 - Draw the structure of a naturally occurring amino...Ch. 21 - Draw the structure of a naturally occurring amino...Ch. 21 - For each amino acid: [1] draw the L enantiomer in...Ch. 21 - For each amino acid: [1] draw the L enantiomer in...Ch. 21 - Draw both enantiomers of each amino acid and label...Ch. 21 - Which of the following Fischer projections...Ch. 21 - For each amino acid: [1] give the name; [2] give...Ch. 21 - For each amino acid: [1] give the name; [2] give...Ch. 21 - (a) Identify the amino acid shown with all...Ch. 21 - Prob. 21.42PCh. 21 - Prob. 21.43PCh. 21 - Draw the structure of the neutral, positively...Ch. 21 - Prob. 21.45PCh. 21 - Prob. 21.46PCh. 21 - (a) Draw the structure of the two possible...Ch. 21 - Prob. 21.48PCh. 21 - Prob. 21.49PCh. 21 - For each tripeptide: [1] draw the structure of the...Ch. 21 - Prob. 21.51PCh. 21 - For each tripeptide: [1] identify the amino acids...Ch. 21 - Prob. 21.53PCh. 21 - Prob. 21.54PCh. 21 - Prob. 21.55PCh. 21 - Prob. 21.56PCh. 21 - Prob. 21.57PCh. 21 - Prob. 21.58PCh. 21 - Prob. 21.59PCh. 21 - Prob. 21.60PCh. 21 - Prob. 21.61PCh. 21 - Prob. 21.62PCh. 21 - What type of intermolecular forces exist between...Ch. 21 - What type of interaction occur at each of the...Ch. 21 - Prob. 21.65PCh. 21 - Draw the structures of the amino acids tyrosine...Ch. 21 - Prob. 21.67PCh. 21 - Prob. 21.68PCh. 21 - Prob. 21.69PCh. 21 - Prob. 21.70PCh. 21 - Prob. 21.71PCh. 21 - Hydrogen bonding stabilizes both the secondary and...Ch. 21 - Prob. 21.73PCh. 21 - Prob. 21.74PCh. 21 - Prob. 21.75PCh. 21 - Prob. 21.76PCh. 21 - What class of enzyme catalyzes each of the...Ch. 21 - What class of enzyme catalyzes each of the...Ch. 21 - Prob. 21.79PCh. 21 - Prob. 21.80PCh. 21 - Prob. 21.81PCh. 21 - What kind of reaction is catalyzed by each of the...Ch. 21 - Prob. 21.83PCh. 21 - How will each of the following changes affect the...Ch. 21 - Prob. 21.85PCh. 21 - Prob. 21.86PCh. 21 - Prob. 21.87PCh. 21 - Prob. 21.88PCh. 21 - Prob. 21.89PCh. 21 - Prob. 21.90PCh. 21 - Prob. 21.91PCh. 21 - Prob. 21.92PCh. 21 - Why must vegetarian diets be carefully balanced?Ch. 21 - Prob. 21.94PCh. 21 - Sometimes an incision is cauterized (burned) to...Ch. 21 - Why is insulin administered by injection instead...Ch. 21 - Prob. 21.97PCh. 21 - The silk produced by a silkworm is a protein with...Ch. 21 - Explain the difference in the mechanism of action...Ch. 21 - Prob. 21.100PCh. 21 - Prob. 21.101CPCh. 21 - Suggest a reason for the following observation....
Additional Science Textbook Solutions
Find more solutions based on key concepts
45. Calculate the mass of nitrogen dissolved at room temperature in an 80.0-L home aquarium. Assume a total pre...
Chemistry: Structure and Properties (2nd Edition)
2. Why is it that the range of resting blood pressures of humans is best represented by a bell-shaped curve co...
Human Biology: Concepts and Current Issues (8th Edition)
6. How can you use the features found in each chapter?
Human Anatomy & Physiology (2nd Edition)
What are the cervical and lumbar enlargements?
Principles of Anatomy and Physiology
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- What special role does the amino acid cysteine have in the peptides vasopressin and oxytocin?arrow_forwardFor the tripeptide GlyAlaCys a. What amino acid is located at the peptides N-terminal end? b. What amino acid is located at the peptides C-terminal end? c. How many peptide bonds are present? d. How many amide linkages are present?arrow_forwardOn complete hydrolysis, a polypeptide gives two alanine, one leucine, one methionine, one phenylalanine, and one valine residue. Partial hydrolysis gives the following fragments: Ala-Phe, Leu-Met, Val-Ala, Phe-Leu. It is known that the first amino acid in the sequence is valine and the last one is methionine. What is the complete sequence of amino acids?arrow_forward
- Identify the R group of the side chain in the following amino acids that results in the side-chain classification indicated in parentheses see Table 19.1: a. tyrosine neutral, polar b. glutamate acidic, polar c. methionine neutral, nonpolar d. histidine basic, polar e. cysteine neutral, polar f. valine neutral, nonpolararrow_forwardIdentifying Amino Acids Which of the following molecules is an amino acid?arrow_forwardUsing both three- and one-letter codes for amino acids, write the structures of all possible peptides containing the following amino acids: (a) Val, Ser, Leu (b) Ser, Leu2, Proarrow_forward
- As we’ve discussed, a peptide bond is made when amino group of one amino acid combines with the carboxylic acid group of another amino acid (releasing a water molecule in the process). The C-N bond formed in this process is called a peptide bond. Peptide bonds have a few properties that might be unexpected. b) Another observation is that although the N-H of the peptide bond is able to serve as a H-bond donor the N atom of the peptide bond does not serve as an effective H-bond acceptor. Provide an explanation for this observation, using Lewis structures, VSEPR theory and/or valence bond theory as appropriate.c) It is also fairly accepted that while proteins undergo dynamic motions and conformational changes, and while R groups can freely rotate about Cα, it is generally not possible to freely rotate around a peptide bond. Please explain this observation, using a picture showing relevant orbitals on relevant atoms (your answer for part (a) might provide a useful basis for your reasoning…arrow_forwardGive detailed Solution with explanation (no need Handwrittenarrow_forwardcircle, identify and name amino acids in the following molecule.arrow_forward
- Please provide explanation using researches or journals. Thank youarrow_forwardDraw the tetrapeptide below out in full chemical structure by attaching the four amino acidsin order (this is an application of the characteristicorganic reaction Formation of an Amide. You can use any chemical notation orcombination of notations to draw your structure, but all bonds and atoms must be shown. Tyr-Cys-Met-Hisarrow_forwardLysine and tryptophan are two amino acids that contain an additional N atom in the R group bonded to the a carbon. While lysine is classified as a basic amino acid because it contains an additional basic N atom, tryptophan is classified as a neutral amino acid. Explain why this difference in classification occurs.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- World of ChemistryChemistryISBN:9780618562763Author:Steven S. ZumdahlPublisher:Houghton Mifflin College DivGeneral, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage Learning
- Organic And Biological ChemistryChemistryISBN:9781305081079Author:STOKER, H. Stephen (howard Stephen)Publisher:Cengage Learning,World of Chemistry, 3rd editionChemistryISBN:9781133109655Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCostePublisher:Brooks / Cole / Cengage LearningChemistry: Matter and ChangeChemistryISBN:9780078746376Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl WistromPublisher:Glencoe/McGraw-Hill School Pub Co
World of Chemistry
Chemistry
ISBN:9780618562763
Author:Steven S. Zumdahl
Publisher:Houghton Mifflin College Div
General, Organic, and Biological Chemistry
Chemistry
ISBN:9781285853918
Author:H. Stephen Stoker
Publisher:Cengage Learning
Organic And Biological Chemistry
Chemistry
ISBN:9781305081079
Author:STOKER, H. Stephen (howard Stephen)
Publisher:Cengage Learning,
World of Chemistry, 3rd edition
Chemistry
ISBN:9781133109655
Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCoste
Publisher:Brooks / Cole / Cengage Learning
Chemistry: Matter and Change
Chemistry
ISBN:9780078746376
Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl Wistrom
Publisher:Glencoe/McGraw-Hill School Pub Co
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY