Proteins fold into complex three-dimensional shapes. The function is dependent upon the structure of the protein and its cellular location. The final shape of the protein is based on the identity of the amino acid side chains of the protein. Many globular proteins are either water soluble or partially water soluble. What type of amino acids would you expect to find on the surface of these proteins? A) nonpolar B) polar neutral C) polar acidic D) polar basic E) any of the polar side chains
Proteins fold into complex three-dimensional shapes. The function is dependent upon the structure of the protein and its cellular location. The final shape of the protein is based on the identity of the amino acid side chains of the protein. Many globular proteins are either water soluble or partially water soluble. What type of amino acids would you expect to find on the surface of these proteins? A) nonpolar B) polar neutral C) polar acidic D) polar basic E) any of the polar side chains
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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Concept explainers
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.
Question
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Transcribed Image Text:**Protein Structure and Surface Amino Acids**
*Question 16.a of 36*
Proteins fold into complex three-dimensional shapes. The function is dependent upon the structure of the protein and its cellular location. The final shape of the protein is based on the identity of the amino acid side chains of the protein.
**Question:**
Many globular proteins are either water soluble or partially water soluble. What type of amino acids would you expect to find on the surface of these proteins?
**Options:**
A) nonpolar
B) polar neutral
C) polar acidic
D) polar basic
E) any of the polar side chains
---
**Explanation:**
This question assesses your understanding of the relationship between protein structure and the chemical properties of the amino acids that compose them. Specifically, it asks you to consider the type of amino acids that are likely to be found on the surface of globular proteins that are water soluble or partially water soluble. The options provided cover different types of amino acids based on their polarity and charge.
For educational purposes, let's delve into each of the provided choices:
A) **Nonpolar:** These amino acids have hydrophobic side chains and are typically found in the interior of proteins, away from water.
B) **Polar Neutral:** These amino acids have side chains that form hydrogen bonds with water but do not carry a charge. They are often found on the protein surface.
C) **Polar Acidic:** These amino acids have side chains that are negatively charged at physiological pH. They can reside on the protein surface, interacting with water or oppositely charged residues.
D) **Polar Basic:** These amino acids have side chains that are positively charged at physiological pH. They can also be found on the protein surface, interacting with water or oppositely charged residues.
E) **Any of the Polar Side Chains:** This suggests considering any amino acid with a polar side chain, which could include neutral, acidic, or basic side chains being present on the surface of globular proteins.
In summary, the most likely answer considering solubility and interaction with the aqueous environment would be E) any of the polar side chains; because polar amino acids, whether neutral, acidic, or basic, facilitate interactions with water, aiding in the protein's solubility.
Transcribed Image Text:**Question 20 of 36**
**What type of interaction would you expect between the R groups, cysteine and cysteine, in tertiary structure?**
A) Hydrophilic
B) Disulfide bonds
C) Hydrophobic / London dispersion
D) Electrostatic interactions
E) Hydrogen bond
---
This question pertains to molecular biology, specifically protein structure. It asks about the type of interaction likely to occur between the side chains (R groups) of the amino acid cysteine in the tertiary structure of a protein.
**Explanation of options:**
- **A) Hydrophilic:** Involves interactions with water molecules, usually between polar or charged side chains.
- **B) Disulfide bonds:** Strong covalent bonds formed between sulfur atoms of two cysteine molecules, crucial for stabilizing protein structure.
- **C) Hydrophobic / London dispersion:** Involves interactions between nonpolar side chains, helping to reduce exposure to water in aqueous environments.
- **D) Electrostatic interactions:** Also known as ionic bonds, occurring between positively and negatively charged side chains.
- **E) Hydrogen bond:** A weak bond between a hydrogen atom and an electronegative atom such as oxygen or nitrogen, common in stabilizing protein secondary structure.
For cysteine, the most relevant interaction would be option B: Disulfide bonds, as these bonds form specifically between the sulfur atoms in the cysteine residues, playing a key role in the stabilization of the protein's tertiary structure.
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