Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction.
Neutral Amino Acids
Amino acids which do not have any charge on them are neutral amino acids.
Globular Protein
The globular proteins refer to the shape of protein specifically spherical in nature apart from spherical form fibrous, disordered and membrane-bound proteins exist. These globular proteins are miscible in water and form a colloidal solution rather than other types which might not exhibit solubility. Many classes of the fold are found in globular proteins, which render them a sphere shape. Globular fold containing proteins usually are referred to by the term globin.
Dimer
Dimers are basic organic compounds, which are derivates of oligomers. It is formed by the combination of two monomers which could potentially be strong or weak and in most cases covalent or intermolecular in nature. Identical monomers are called homodimer, the non-identical dimers are called heterodimer. The method by which dimers are formed is known as “dimerization”.
Dipeptide
A dipeptide is considered a mixture of two distinct amino acids. Since the amino acids are distinct, based on their composition, two dipeptide's isomers can be produced. Various dipeptides are biologically essential and are therefore crucial to industry.
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction.
Explain why that's the case for EACH of the bonds.
I.e
Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than Sulfur-arene interactions, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than Anion-π interactions, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than Chalcogen bonds, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than X-H-π interactions, even though n→π* is the weaker interaction.
![Author Manuscript
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Newberry and Raines
မှာ
Total Energy per 100 Residues
(kcal/mol)
10
8
TT-TT Interactions
C5 Hydrogen bonds
n→* Interactions
C-HO Hydrogen bonds
Anion-77
Cation-77 interactions
Sulfur-arene interactions
Page 20
ACS Chem Biol Author manuscript, available in PMC 2020 February 01.
interactions
Chalcogen bonds
X-H77 Interactions
Figure 3.
Bar graph of the
estimated enthalpic contribution of secondary interactions the
conformational stability of globular proteins. Black bars, interactions of the main chain
(Figure 1); gray bars, interactions involving side chains (Figure 2). Data are from Table 1.
The sum of the energies is -27 kcal/mol per 100 residues.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fda3085ce-1e06-4366-ab49-1fc5094c490f%2Fd3eec7b5-2a90-4cea-8523-4bc8ab9dbd5b%2F87gqkdw_processed.jpeg&w=3840&q=75)
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Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction.
Explain why that's the case for EACH of the bonds.
Why n→π* interactions contribute more to the overall stabilization of the protein than Sulfur-arene interactions, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than Anion-π interactions, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than Chalcogen bonds, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than X-H-π interactions, even though n→π* is the weaker interaction.
![Author Manuscript
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Newberry and Raines
Table 1.
Estimated Frequency and Energy of Secondary Forces in Protein Folding
Interaction
* Interactions
C-H--O Hydrogen bonds
*-* Interactions
CS Hydrogen bonds
Cation- interactions
Sulfur-arene interactions
Anion- interactions
Chalcogen bonds
X-H- Interactions
Approximate Frequency per 100 Residues
3357
10³1
5111
583
1-2⁹4
2-3130
1-2125
1102
Approximate Energy (kcal/mol)
0.2569
0-141,42
0.5-1.5117-119
0.25-1.583
0.5-285
0.3-0.5133,134
0.5124
0.64140
0.35143
Page 21
*Preference is given to experimental measurements a proteins and peptides. Computational values are used in the absence of experimental data.
Frequency per 100 residues was estimated by multiplying the frequency of relevant residues95 by the fraction of those residues that engage in the
interaction.
ACS Chem Biol Author manuscript, available in PMC 2020 February 01.](https://content.bartleby.com/qna-images/question/da3085ce-1e06-4366-ab49-1fc5094c490f/79178ce7-8916-41fb-8a4b-53ffe6b65767/y0s5so_thumbnail.jpeg)
![Author Manuscript
Author Manuscript
Author Manuscript
Author Manuscript
Newberry and Raines
မှာ
Total Energy per 100 Residues
(kcal/mol)
10
8
TT-TT Interactions
C5 Hydrogen bonds
n→* Interactions
C-HO Hydrogen bonds
Anion-77
Cation-77 interactions
Sulfur-arene interactions
Page 20
ACS Chem Biol Author manuscript, available in PMC 2020 February 01.
interactions
Chalcogen bonds
X-H77 Interactions
Figure 3.
Bar graph of the
estimated enthalpic contribution of secondary interactions the
conformational stability of globular proteins. Black bars, interactions of the main chain
(Figure 1); gray bars, interactions involving side chains (Figure 2). Data are from Table 1.
The sum of the energies is -27 kcal/mol per 100 residues.](https://content.bartleby.com/qna-images/question/da3085ce-1e06-4366-ab49-1fc5094c490f/79178ce7-8916-41fb-8a4b-53ffe6b65767/3w5k0l_thumbnail.jpeg)
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