Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Edition (8th Edition)
Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Edition (8th Edition)
8th Edition
ISBN: 9780134218328
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
bartleby

Concept explainers

bartleby

Videos

Question
Book Icon
Chapter 18, Problem 18.98CP

(a)

Interpretation Introduction

Interpretation:

The influences on the tertiary structure for each of the amino acid given has to be identified based on hydrophobic interaction, hydrogen bonding , formation of salt bridges, covalent bonding or combinations.

Concept introduction:

Tertiary structure is the noncovalent interaction that holds the single protein in a three dimensional shape takes place primarily between the disulphide bonds and side chain thiol groups.

The main interaction that takes place in the tertiary structure of protein are

  • Hydrophobic interaction
  • Hydrogen bonds and R side chain
  • Ionic interaction and
  • Disulphide interaction.

Hydrogen bonding is the electrostatic force of attraction between hydrogen and the electronegative atom.

(b)

Interpretation Introduction

Interpretation:

The influences on the tertiary structure for each of the amino acid given has to be identified based on hydrophobic interaction, hydrogen bonding , formation of salt bridges, covalent bonding or combinations.

Concept introduction:

Tertiary structure is the noncovalent interaction that holds the single protein in a three dimensional shape takes place primarily between the disulphide bonds and side chain thiol groups.

The main interaction that takes place in the tertiary structure of protein are

  • Hydrophobic interaction
  • Hydrogen bonds and R side chain
  • Ionic interaction and
  • Disulphide interaction.

Disulfide bridges are covalent S-S bond formed between these side chains that can join two separate peptide chain or cause a loop in a single peptide chain.

(c)

Interpretation Introduction

Interpretation:

The influences on the tertiary structure for each of the amino acid given has to be identified based on hydrophobic interaction, hydrogen bonding , formation of salt bridges, covalent bonding or combinations.

Concept introduction:

Tertiary structure is the noncovalent interaction that holds the single protein in a three dimensional shape takes place primarily between the disulphide bonds and side chain thiol groups.

The main interaction that takes place in the tertiary structure of protein are

  • Hydrophobic interaction
  • Hydrogen bonds and R side chain
  • Ionic interaction and
  • Disulphide interaction.

Hydrogen bonding is the electrostatic force of attraction between hydrogen and the electronegative atom.

(d)

Interpretation Introduction

Interpretation:

The influences on the tertiary structure for each of the amino acid given has to be identified based on hydrophobic interaction, hydrogen bonding , formation of salt bridges, covalent bonding or combinations.

Concept introduction:

Tertiary structure is the noncovalent interaction that holds the single protein in a three dimensional shape takes place primarily between the disulphide bonds and side chain thiol groups.

The main interaction that takes place in the tertiary structure of protein are

  • Hydrophobic interaction
  • Hydrogen bonds and R side chain
  • Ionic interaction and
  • Disulphide interaction.

The acidic and basic side chains attract each other giving rise to salt bridge.

(e)

Interpretation Introduction

Interpretation:

The influences on the tertiary structure for each of the amino acid given has to be identified based on hydrophobic interaction, hydrogen bonding , formation of salt bridges, covalent bonding or combinations.

Concept introduction:

Tertiary structure is the noncovalent interaction that holds the single protein in a three dimensional shape takes place primarily between the disulfide bonds and side chain thiol groups.

The main interaction that takes place in the tertiary structure of protein are

  • Hydrophobic interaction
  • Hydrogen bonds and R side chain
  • Ionic interaction and
  • Disulphide interaction.

Hydrocarbon side chain are attracted to each other by dispersion forces caused as a result of uneven distribution of electrons give rise to hydrophobic interaction.

(f)

Interpretation Introduction

Interpretation:

The influences on the tertiary structure for each of the amino acid given has to be identified based on hydrophobic interaction, hydrogen bonding , formation of salt bridges, covalent bonding or combinations.

Concept introduction:

Tertiary structure is the noncovalent interaction that holds the single protein in a three dimensional shape takes place primarily between the disulfide bonds and side chain thiol groups.

The main interaction that takes place in the tertiary structure of protein are

  • Hydrophobic interaction
  • Hydrogen bonds and R side chain
  • Ionic interaction and
  • Disulphide interaction.

Hydrocarbon side chain are attracted to each other by dispersion forces caused as a result of uneven distribution of electrons give rise to hydrophobic interaction.

(g)

Interpretation Introduction

Interpretation:

The influences on the tertiary structure for each of the amino acid given has to be identified based on hydrophobic interaction, hydrogen bonding , formation of salt bridges, covalent bonding or combinations.

Concept introduction:

Tertiary structure is the noncovalent interaction that holds the single protein in a three dimensional shape takes place primarily between the disulphide bonds and side chain thiol groups.

The main interaction that takes place in the tertiary structure of protein are

  • Hydrophobic interaction
  • Hydrogen bonds and R side chain
  • Ionic interaction and
  • Disulphide interaction.

Hydrocarbon side chain are attracted to each other by dispersion forces caused as a result of uneven distribution of electrons give rise to hydrophobic interaction.

(h)

Interpretation Introduction

Interpretation:

The influences on the tertiary structure for each of the amino acid given has to be identified based on hydrophobic interaction, hydrogen bonding , formation of salt bridges, covalent bonding or combinations.

Concept introduction:

Tertiary structure is the noncovalent interaction that holds the single protein in a three dimensional shape takes place primarily between the disulphide bonds and side chain thiol groups.

The main interaction that takes place in the tertiary structure of protein are

  • Hydrophobic interaction
  • Hydrogen bonds and R side chain
  • Ionic interaction and
  • Disulfide interaction.

Hydrocarbon side chain is attracted to each other by dispersion forces caused as a result of uneven distribution of electrons give rise to hydrophobic interaction.

Blurred answer
Students have asked these similar questions
For the amino acids listed below, what tertiary/quaternary interaction can each of the amino acids participate in? 1)Alanine 2)Asparagine 3) Aspartic Acid 4) Arginine
Describe in detail the composition and structure of peptidoglycan. Why does peptidoglycan contain the unusual d-isomers of alanine and glutamic acid rather than the l-isomers observed in proteins?
Given this short polypeptide: Met-Ala-Gly-Ser A) Which is the amino terminal amino acid? B) How many amino acids are in this polypeptide? C) How many peptide bonds are in this polypeptide? D) Which amino acid has the smallest side chain? E) Which amino acid contains sulfur?

Chapter 18 Solutions

Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Edition (8th Edition)

Ch. 18.3 - Prob. 18.11PCh. 18.3 - Prob. 18.12PCh. 18.4 - The proteins collagen, bovine insulin, and human...Ch. 18.4 - Prob. 18.2CIAPCh. 18.4 - Prob. 18.13PCh. 18.4 - Prob. 18.14PCh. 18.5 - Valine is an amino acid with a nonpolar side...Ch. 18.5 - Tripeptides are composed of three amino acids...Ch. 18.5 - Prob. 18.17PCh. 18.5 - Identify the amino acids in the following...Ch. 18.5 - Prob. 18.19PCh. 18.5 - Prob. 18.3CIAPCh. 18.5 - Prob. 18.4CIAPCh. 18.5 - Two of the most complete (balanced) proteins...Ch. 18.6 - Prob. 18.6CIAPCh. 18.6 - Prob. 18.7CIAPCh. 18.6 - (a)What atoms are present in a planar unit in a...Ch. 18.6 - Prob. 18.21PCh. 18.6 - Prob. 18.22PCh. 18.7 - Prob. 18.23PCh. 18.7 - Prob. 18.24PCh. 18.7 - Complete the following two sentences with either...Ch. 18.7 - Prob. 18.26KCPCh. 18.8 - Which of the following pairs of amino acids can...Ch. 18.8 - Look at Table 18.3 and identify the type of...Ch. 18.8 - In Figure 18.3, identify the amino acids that have...Ch. 18.8 - Prob. 18.30PCh. 18.9 - Prob. 18.31PCh. 18.10 - Another endoprotease is trypsin. Trypsin...Ch. 18.10 - Prob. 18.33PCh. 18.10 - Prob. 18.8CIAPCh. 18.10 - Prob. 18.9CIAPCh. 18 - Draw the structure of the following amino acids,...Ch. 18 - Prob. 18.35UKCCh. 18 - Prob. 18.36UKCCh. 18 - Prob. 18.37UKCCh. 18 - Prob. 18.38UKCCh. 18 - Threonine has two chiral centers. Draw L-threonine...Ch. 18 - Name four biological functions of proteins in the...Ch. 18 - Prob. 18.41APCh. 18 - Prob. 18.42APCh. 18 - Prob. 18.43APCh. 18 - Prob. 18.44APCh. 18 - Prob. 18.45APCh. 18 - Prob. 18.46APCh. 18 - Prob. 18.47APCh. 18 - Draw leucine and identify any chiral carbon atoms...Ch. 18 - Prob. 18.49APCh. 18 - Prob. 18.50APCh. 18 - Is histidine hydrophilic or hydrophobic? Explain...Ch. 18 - Prob. 18.52APCh. 18 - At neutral pH, which of the following amino acids...Ch. 18 - Prob. 18.54APCh. 18 - Prob. 18.55APCh. 18 - Prob. 18.56APCh. 18 - Prob. 18.57APCh. 18 - Proteins are usually least soluble in water at...Ch. 18 - Prob. 18.59APCh. 18 - Prob. 18.60APCh. 18 - Prob. 18.61APCh. 18 - Prob. 18.62APCh. 18 - Prob. 18.63APCh. 18 - (a)Identify the amino acids present in the peptide...Ch. 18 - Prob. 18.65APCh. 18 - Prob. 18.66APCh. 18 - Prob. 18.67APCh. 18 - Prob. 18.68APCh. 18 - Prob. 18.69APCh. 18 - Prob. 18.70APCh. 18 - Prob. 18.71APCh. 18 - Prob. 18.72APCh. 18 - Prob. 18.73APCh. 18 - Prob. 18.74APCh. 18 - Prob. 18.75APCh. 18 - What kind of bond would you expect between chains...Ch. 18 - Is the bond formed between each pair in Problem...Ch. 18 - Prob. 18.78APCh. 18 - Prob. 18.79APCh. 18 - Prob. 18.80APCh. 18 - Prob. 18.81APCh. 18 - Prob. 18.82APCh. 18 - Prob. 18.83APCh. 18 - Prob. 18.84APCh. 18 - Prob. 18.85APCh. 18 - Prob. 18.86APCh. 18 - Prob. 18.87APCh. 18 - Prob. 18.88APCh. 18 - Give an example of a protein that has quaternary...Ch. 18 - Prob. 18.90APCh. 18 - Prob. 18.91APCh. 18 - Prob. 18.92APCh. 18 - Prob. 18.93APCh. 18 - Prob. 18.94APCh. 18 - Prob. 18.95APCh. 18 - Prob. 18.96APCh. 18 - Prob. 18.97APCh. 18 - Prob. 18.98CPCh. 18 - Prob. 18.99CPCh. 18 - Prob. 18.100CPCh. 18 - Prob. 18.101CPCh. 18 - Prob. 18.102CPCh. 18 - Prob. 18.103CPCh. 18 - Prob. 18.104CPCh. 18 - Prob. 18.105CPCh. 18 - Prob. 18.106CPCh. 18 - Prob. 18.107CPCh. 18 - Prob. 18.108CPCh. 18 - Prob. 18.109GPCh. 18 - Prob. 18.110GPCh. 18 - Prob. 18.111GPCh. 18 - Prob. 18.112GP
Knowledge Booster
Background pattern image
Biochemistry
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
SEE MORE QUESTIONS
Recommended textbooks for you
Text book image
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Text book image
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Text book image
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Text book image
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Text book image
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license