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
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Chapter 18, Problem 18.86AP
Interpretation Introduction

Interpretation:

How hydrophobic interaction stabilizes the tertiary and quaternary structure of protein is to be identified.

Concept introduction:

Tertiary protein structure is the folding of a single protein into a specific three dimensional shape, held by noncovalent interaction between the side chains.

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.

R (Alkyl or aryl) groups are attracted to each other by dispersion forces due to the uneven distribution of electrons are referred to as hydrophobic interaction.

Interpretation Introduction

Interpretation:

How salt bridges stabilize the tertiary and quaternary structure of protein is to be identified.

Concept introduction:

Tertiary protein structure is the folding of a single protein into a specific three dimensional shape, held by noncovalent interaction between the side chains.

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.

Ionic acidic and basic side chain results in salt bridge interaction.

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Students have asked these similar questions
How do the following interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.(a) Side-chain hydrogen bonding(b) Disulfide bonds
Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure of a protein. What types of interactions stabilize each type of structure?(a) The polypeptide chain has a number of bends and twists, resulting in a compact structure.(b) The polypeptide backbone forms a right-handed coil.(c) The four polypeptide chains are arranged in a spherical shape.
Generally speaking, what two considerations determine whether a specific dihedral angle will be permitted to exist in a protein?

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
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