When pure crystalline amino acids are heated, decomposition generally occurs before the solid melts. Account for this observation. (Hint: Crystalline amino acids exist as \(\mathbf{H}_{3} \mathrm{NCRHCOO}^{-}\) called zwitterions.)

Short Answer

Expert verified
In conclusion, the decomposition of pure crystalline amino acids before melting when heated is due to their zwitterionic structure (\(\mathrm{H}_{3}\mathrm{NCRHCOO}^{-}\)). The strong ionic bonds formed in the crystal lattice require more energy to break than the covalent bonds within the amino acid molecules. As a result, the covalent bonds break first upon heating, causing decomposition before the solid amino acids can melt into a liquid state.

Step by step solution

01

Understanding zwitterions

A zwitterion is a molecule with both positive and negative charges, but with an overall net charge of zero. In the case of amino acids, the zwitterionic form has a positively charged amino group (\(\mathrm{NH}_{3}^{+}\)) and a negatively charged carboxylate group (\(\mathrm{COO}^{-}\)). This unique structure allows amino acids to stabilize through strong electrostatic interactions between the oppositely charged groups.
02

Explaining the stability of crystalline amino acids

In crystalline amino acids, the zwitterionic form allows the molecules to arrange themselves in a stable lattice structure. The oppositely charged groups in each amino acid molecule form strong ionic bonds with each other, leading to the formation of a highly stable crystal lattice.
03

Effects of heating on crystalline amino acids

When the crystalline amino acids are heated, the thermal energy causes the molecules to vibrate and eventually break the ionic bonds in the crystal lattice. However, since the zwitterionic structure of amino acids involves relatively strong ionic bonds, it requires a significant amount of energy to break these bonds. This energy is typically higher than the energy needed to break the covalent bonds within the molecule itself.
04

Decomposition before melting

As the crystalline amino acids are heated, the covalent bonds within the amino acids begin to break first due to the lower energy required. This leads to the decomposition of the amino acid molecules into simpler compounds before the ionic bonds in the crystal lattice have a chance to break completely. Consequently, decomposition occurs before the solid amino acids have an opportunity to melt into a liquid state. In conclusion, the observation that pure crystalline amino acids decompose before melting when heated can be attributed to their zwitterionic structure, which creates strong ionic bonds in the crystal lattice. The energy required to break these ionic bonds is generally higher than the energy needed to break the covalent bonds within the amino acid molecules, resulting in decomposition prior to melting.

Unlock Step-by-Step Solutions & Ace Your Exams!

  • Full Textbook Solutions

    Get detailed explanations and key concepts

  • Unlimited Al creation

    Al flashcards, explanations, exams and more...

  • Ads-free access

    To over 500 millions flashcards

  • Money-back guarantee

    We refund you if you fail your exam.

Over 30 million students worldwide already upgrade their learning with Vaia!

One App. One Place for Learning.

All the tools & learning materials you need for study success - in one app.

Get started for free

Most popular questions from this chapter

In glycine, the carboxylic acid group has \(K_{\mathrm{a}}=4.3 \times 10^{-3}\) and the amino group has \(K_{b}=6.0 \times 10^{-5} .\) Use these equilibrium constant values to calculate the cquilibrium constants for the following. a. \(^{+} \mathrm{H}_{3} \mathrm{NCH}_{2} \mathrm{CO}_{2}^{-}+\mathrm{H}_{2} \mathrm{O} \rightleftharpoons \mathrm{H}_{2} \mathrm{NCH}_{2} \mathrm{CO}_{2}^{-}+\mathrm{H}_{3} \mathrm{O}^{+}\) b. \(\mathrm{H}_{2} \mathrm{NCH}_{2} \mathrm{CO}_{2}^{-}+\mathrm{H}_{2} \mathrm{O} \rightleftharpoons \mathrm{H}_{2} \mathrm{NCH}_{2} \mathrm{CO}_{2} \mathrm{H}+\mathrm{OH}^{-}\) c. \(\mathbf{H}_{3} \mathrm{NCH}_{2} \mathrm{CO}_{2} \mathrm{H} \rightleftharpoons 2 \mathrm{H}^{+}+\mathrm{H}_{2} \mathrm{NCH}_{2} \mathrm{CO}_{2}^{-}\)

If you had a group of hydrocarbons, what structural features would you look at to rank the hydrocarbons in order of increasing boiling point?

In the presence of light, chlorine can substitute for one (or more) of the hydrogens in an alkane. For the following reactions, draw the possible monochlorination products. a. 2,2 -dimethylpropane \(+\mathrm{Cl}_{2} \stackrel{\mathrm{hv}}{\longrightarrow}\) b. 1,3 -dimethylcyclobutane \(+\mathrm{Cl}_{2} \stackrel{\mathrm{hv}}{\longrightarrow}\) c. 2,3 -dimethylbutane \(+\mathrm{Cl}_{2} \stackrel{\mathrm{hv}}{\longrightarrow}\)

The codons (words) in DNA (that specify which amino acid should be at a particular point in a protein) are three bases long. How many such three- letter words can be made from the four bases adenine, cytosine, guanine, and thymine?

For each of the following, fill in the blank with the correct response(s). All of the following pertain to nucleic acids. a. The substance in the nucleus of the cell that stores and transmits genetic information is DNA, which stands for _________ b. The basic repeating monomer units of DNA and RNA are called _______ c. The pentose deoxyribose is found in DNA, whereas ________is found in RNA. d. The basic linkage in DNA or RNA between the sugar molecule and phosphoric acid is a phosphate _______ linkage. e. The bases on opposite strands of DNA are said to be __________ to each other, which means the bases fit together specifically by hydrogen bonding to one another. f. In a strand of normal DNA, the base__________is always always found paired with cytosine. g. A given segment of the DNA molecule, which contains the molecular coding for a specific protein to be synthesized, is referred to as a _______ h. During protein synthesis, ______RNA molecules attach to and transport specific amino acids to the appropriate position on the pattern provided by _______RNA molecules. i. The codes specified by ________are responsible for assembling the correct primary structure of proteins.

See all solutions

Recommended explanations on Chemistry Textbooks

View all explanations

What do you think about this solution?

We value your feedback to improve our textbook solutions.

Study anywhere. Anytime. Across all devices.

Sign-up for free