Chapter 15, Problem 15.101P

(a)

Interpretation Introduction

Interpretation:

The amino acid that possesses the given $\text{R}$ group has to be named and the force that arises in the interaction of those groups has to be given.

  ${\text{-CH}}_{\text{2}}{\text{-SH with SH-CH}}_{\text{2}}\text{-}$

Concept Introduction:

Intermolecular forces:

The weaker forces that are formed between the molecules to bind together in groups are known as intermolecular forces or secondary bonds.  The intermolecular is generally defined by the term Vanderwaal forces.

Intermolecular forces in proteins:

• The back bone of the protein chain forms by covalent peptide bonds.
• The hydrogen bonds between $\text{C=O}$ of one peptide bond and $\text{N-H}$ of another peptide bond forms helical or sheet-like segments.
• Polar and ionic side chains protrude into the surrounding cell fluid interacting with water through ion-dipole forces and hydrogen bonding.
• Non-polar side chains interact through dispersion forces.
• The $\text{-SH}$ ends of two cysteine side chains forms a covalent $\text{-S-S-}$ bond, a disulfide bridge.
• Salt linkage is formed by oppositely charged ends of side chains ${\text{-COO}}^{\text{-}}$ and ${\text{-NH}}_{\text{3}}{}^{\text{+}}$.
• The hydrogen bonds between side chains keeps the distant chain portions nearer.

(b)

Interpretation Introduction

Interpretation:

The amino acid that possesses the given $\text{R}$ group has to be named and the force that arises in the interaction of those groups has to be given.

  $\text{-}{\left({\text{CH}}_{\text{2}}\right)}_{\text{4}}{\text{-NH}}_{\text{3}}^{\text{+}}\text{ with }\text{O}\text{-}\stackrel{\stackrel{\text{O}}{\text{||}}}{\text{C}}{\text{-CH}}_{\text{2}}\text{-}$

Concept Introduction:

Intermolecular forces:

The weaker forces that are formed between the molecules to bind together in groups are known as intermolecular forces or secondary bonds.  The intermolecular is generally defined by the term Vanderwaal forces.

Intermolecular forces in proteins:

• The back bone of the protein chain forms by covalent peptide bonds.
• The hydrogen bonds between $\text{C=O}$ of one peptide bond and $\text{N-H}$ of another peptide bond forms helical or sheet-like segments.
• Polar and ionic side chains protrude into the surrounding cell fluid interacting with water through ion-dipole forces and hydrogen bonding.
• Non-polar side chains interact through dispersion forces.
• The $\text{-SH}$ ends of two cysteine side chains forms a covalent $\text{-S-S-}$ bond, a disulfide bridge.
• Salt linkage is formed by oppositely charged ends of side chains ${\text{-COO}}^{\text{-}}$ and ${\text{-NH}}_{\text{3}}{}^{\text{+}}$.
• The hydrogen bonds between side chains keeps the distant chain portions nearer.

(c)

Interpretation Introduction

Interpretation:

The amino acid that possesses the given $\text{R}$ group has to be named and the force that arises in the interaction of that groups has to be given.

  ${\text{ -CH}}_{\text{2}}\text{-}\stackrel{\stackrel{\text{O}}{\text{||}}}{\text{C}}{\text{-NH}}_{\text{2}}{\text{- with HO-CH}}_{\text{2}}\text{-}$

Concept Introduction:

Intermolecular forces:

The weaker forces that are formed between the molecules to bind together in groups are known as intermolecular forces or secondary bonds.  The intermolecular is generally defined by the term Vanderwaal forces.

Intermolecular forces in proteins:

• The back bone of the protein chain forms by covalent peptide bonds.
• The hydrogen bonds between $\text{C=O}$ of one peptide bond and $\text{N-H}$ of another peptide bond forms helical or sheet-like segments.
• Polar and ionic side chains protrude into the surrounding cell fluid interacting with water through ion-dipole forces and hydrogen bonding.
• Non-polar side chains interact through dispersion forces.
• The $\text{-SH}$ ends of two cysteine side chains forms a covalent $\text{-S-S-}$ bond, a disulfide bridge.
• Salt linkage is formed by oppositely charged ends of side chains ${\text{-COO}}^{\text{-}}$ and ${\text{-NH}}_{\text{3}}{}^{\text{+}}$.
• The hydrogen bonds between side chains keeps the distant chain portions nearer.

(d)

Interpretation Introduction

Interpretation:

The amino acid that possesses the given $\text{R}$ group has to be named and the force that arises in the interaction of that groups has to be given.

Concept Introduction:

Intermolecular forces:

The weaker forces that are formed between the molecules to bind together in groups are known as intermolecular forces or secondary bonds.  The intermolecular is generally defined by the term Vanderwaal forces.

Intermolecular forces in proteins:

• The back bone of the protein chain forms by covalent peptide bonds.
• The hydrogen bonds between $\text{C=O}$ of one peptide bond and $\text{N-H}$ of another peptide bond forms helical or sheet-like segments.
• Polar and ionic side chains protrude into the surrounding cell fluid interacting with water through ion-dipole forces and hydrogen bonding.
• Non-polar side chains interact through dispersion forces.
• The $\text{-SH}$ ends of two cysteine side chains forms a covalent $\text{-S-S-}$ bond, a disulfide bridge.
• Salt linkage is formed by oppositely charged ends of side chains ${\text{-COO}}^{\text{-}}$ and ${\text{-NH}}_{\text{3}}{}^{\text{+}}$.
• The hydrogen bonds between side chains keeps the distant chain portions nearer.