Biology (MindTap Course List)
11th Edition
ISBN: 9781337392938
Author: Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 3, Problem 12TYU
PREDICT Do any of the amino acid side groups shown below have the potential to form an ionic bond with any of the other side groups shown? If so, which pair(s) could form such an association?
(a) —CH3
(b) —CH2 — COO—
(c) —CH2 — CH2 — NH3+
(d) —CH2 — CH2 — COO—
(e) —CH2 — OH
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
The amino acid arginine ionizes according to the following scheme:
NH,
NH2
NH2
H
NH,
C=N
C=N
C=N
C=N-H
pk = 2.17
-H
pK. = 8.99
-H
pK = 125
-H*
H.
NH
NH
NH
NH
H (CH,)a
H (CH),
+H*
(CH)a
(CH,)a
H,N-C-coo-
+H*
+H*
H-N*-C-COOH
H-N-C-Co-
H,N-C-co-
H.
нн
H.
H
II
II
IV
(a) Calculate the isoelectric point of arginine. You can neglect contributions
from form I. Why?
(b) Calculate the average charge on arginine when pH = 9.20. (Hìnt: Find
the average charge for each ionizable group and sum these together.)
(c) Is the value of average charge you calculated in part b reasonable, given
the pl you calculated in part a? Explain your answer.
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).
Chemistry
Consider a protein with a beta conformation sequence EAGQVHRGP a) Which residue(s) can be substituted by N without affecting the conformation? b) Which residue(s) can be substituted by D without affecting the conformation? c) Which residue(s) cannot be substituted without affecting the conformation?
Chapter 3 Solutions
Biology (MindTap Course List)
Ch. 3.1 - Describe the properties of carbon that make it the...Ch. 3.1 - Define the term isomer and distinguish among the...Ch. 3.1 - Identify the major functional groups present in...Ch. 3.1 - Explain the relationship between polymers and...Ch. 3.1 - What are some of the ways that the features of...Ch. 3.1 - Prob. 2CCh. 3.1 - Prob. 3CCh. 3.1 - Prob. 4CCh. 3.1 - Prob. 5CCh. 3.2 - Distinguish among monosaccharides, disaccharides,...
Ch. 3.2 - VISUALIZE Draw simple sketches comparing the...Ch. 3.3 - Distinguish among fats, phospholipids, and...Ch. 3.3 - Prob. 1CCh. 3.3 - Explain why the structure of phospholipids enables...Ch. 3.4 - Give an overall description of the structure and...Ch. 3.4 - Prob. 8LOCh. 3.4 - Distinguish among the four levels of organization...Ch. 3.4 - Prob. 1CCh. 3.4 - Prob. 2CCh. 3.5 - Describe the components of a nucleotide. Name some...Ch. 3.5 - VISUALIZE Sketch a pyrimidine nucleotide subunit...Ch. 3.6 - Compare the functions and chemical compositions of...Ch. 3.6 - How can you distinguish a pentose sugar from a...Ch. 3 - Prob. 1TYUCh. 3 - VISUALIZE The structures depicted are (a)...Ch. 3 - Prob. 3TYUCh. 3 - The synthetic process by which monomers are...Ch. 3 - A monosaccharide designated as an aldehyde sugar...Ch. 3 - Structural polysaccharides typically (a) have...Ch. 3 - Saturated fatty acids are so named because they...Ch. 3 - Fatty acids in phospholipids and triacylglycerols...Ch. 3 - Which of the following levels of protein structure...Ch. 3 - Which of the following associations between R...Ch. 3 - Each phosphodiester linkage in DNA or RNA includes...Ch. 3 - PREDICT Do any of the amino acid side groups shown...Ch. 3 - PREDICT Like oxygen, sulfur forms two covalent...Ch. 3 - Hydrogen bonds and van der Waals interactions are...Ch. 3 - EVOLUTION LINK In what ways are all species alike...Ch. 3 - EVOLUTION LINK The total number of possible amino...Ch. 3 - EVOLUTION LINK Each amino acid could potentially...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- What charged groups are present in glutamate at a pH = 7? OA) 1 × NH3 + B) 1 × COO™ O C) 1 × NH3* and 1 × COO- D) 2 × NH3 and 1 × COO E) 1× NH3 and 2 × COO- OF) Nonearrow_forward(1) (2) (3) (4) (5) (6) (8) (9) (10) E Which of the following residues would be most likely to make contact with the aqueous medium? (A) Lysine (B) Glycine (12) The native state of a protein is the conformation that is the (A) (8) The (A) (B) (B) When an atom or ion is reduced, its oxidation number (A) Decreases (8) Increases Ribose is an example of a (A) Pentose Hexose (A) (8) Palmitate (16:0) is a/an Saturated Unsaturated (7) A certain unfavorable process has an associated standard free energy (AG) of 38 kJ/mol. To which reaction could it be coupled to make it favorable? ATP+H₂O → ADP + P ATP + H₂O → AMP + PP, Neither one (A) (B) (C) Least Most Lesser Greater (A) (8) (A) the value of ko, the more efficient the enzyme will be. (8) Generally, if the concentration of ATP is low, then Gluconeogenesis Glycolysis (A) (8) sugar. In the first step of the citric acid cycle, Acetyl CoA Pyruvate fatty acid. (AG"=-32 kl/mol) (AG"=-45kl/mol) Under conditions when glycogen synthesis is favored,…arrow_forwardWhich of the following shows the reaction by which valine and leucine form a peptide bond H. H. H O -COO H2N-C-C-NH- C- C-OH + HO CH2 CH,SH ČH3 А. C. CH(CH)2 H. HN-C-C-NH-C- C-OH H,N-CH-C- + H,O HC-C-H CH2 CH2 H CH3 CH H,C-C-H CH(CH3)2 CH В. D.arrow_forward
- What charged groups are present in lysine at a pH = 7? O A) 1 × NH3¹ B) 1 x COO OC) 1× NH3+ and 1 x COO- Jay OD) 2 × NH3 and 1 × COO- + OE) 1 × NH3+ and 2 × COO- O F) Nonearrow_forward1. Examine the synthetic glycoprotein, Molecule A, shown below: Protein- OH OH OH OH OH ÓH OH Molecule A OH Draw the structures of the products obtained when Molecule A reacts under the following conditions. Justify your answer. If no reaction occurs, explain why. The monosaccharide rings that have not reacted may be represented by an “R" group. Mechanisms are not required. (а) Ammonium Carbonate, 5 days. (b) Excess Sodium Periodate. (c) 2,3-dinitrophenyl hydrazine under reductive amination conditions. NO2 O2N. „NHNH2 2,3-dinitrophenyl hydrazinearrow_forwardWhat types of interactions are possible between the side chains of the polypeptide shown below? Select all that apply: H. H H O Disulfide bonds Hydrogen bonds O lonic bonds Hydrophobic interactions ......arrow_forward
- Identify what type of chemical interactions is involved in the following side chains of the peptide chain below: 3 H-Q 0-H 5. OH OH CH, 6. 9. 4. -- CH, 2. 200 CH, 12 CH CH, -NH,0-C 4 1. 15 3. CH.-OH O CH. 17 18 The following choices can be applied for the following type of chemical interactions. 20 21 Write: AB - if it is a salt bridge or ionic bond CD - if it's a H-bonding 23 24 EF - if it's a hydrophobic interactions GH - if it's a disulfide bondarrow_forwardDescribe the amino acid illustrated here (Identify the following amino acid (at pH = 7.0): (COO-)–CH(NH3+)–CH2–CH2–CH2–CH2–(NH3+)) (at pH = 7.0). it is a polar, negatively-charged amino acid it is a non-polar, negatively-charged amino acid it is a polar, positively-charged amino acid it is a non-polar, positively-charged amino acid it is a non-polar, uncharged amino acidarrow_forwardWhich of the following are saponifiable lipids? (Recall that ester bonds are broken by base hydrolysis.)(a) Progesterone (b) Glyceryl trioleate(c) A sphingomyelin (d) Prostaglandin E1(e) A cerebroside (f) A lecithinarrow_forward
- asaparrow_forward2) What is glycoside ? In neutral and basic solutions, glycosides do not show mutarotation. However, if the solutions are made acidic, glycosides show mutarotation. Explain why? And write a mutarotation mechanism.arrow_forwardFor each of the following pairs of amino acids, identify the strongest type of intermolecular forces involved when the side chains interact. Explain in terms of the chemical structures of the amino acid side chains. Use the following list: disulfide bridge, hydrogen bonding, hydrophobic interaction, or salt bridge. a) D and H b) C and C c) L and A d) G and S e) N and Tarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage Learning
Biology (MindTap Course List)
Biology
ISBN:9781337392938
Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher:Cengage Learning
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license