macromolecular building blocks Flashcards
Describe the composition of macromolecular building blocks
Macromolecular building blocks often contain phosphorus (P) and/or sulfur (S) in addition to carbon (C), nitrogen (N), oxygen (O), and hydrogen (H).
Define the role of amino acids in biochemistry.
Amino acids are the building blocks of proteins.
How do nucleotides contribute to genetic material?
Nucleotides make up DNA and RNA.
What is the major component of lipids?
The major component of lipids is hydrocarbons.
Explain the relationship between carbohydrates and polysaccharides.
Carbohydrates are the building blocks that make up polysaccharides, glycans, and more.
Describe the structure of an amino acid.
An amino acid consists of an amino group and an acidic group linked by a central carbon (α carbon), which is tetrahedral and has single bonds to four surrounding atoms, including a variable side chain (R)
How many variations of amino acids exist?
There are 20 variations of amino acids, leading to 20 different amino acids.
List the elements that are fundamental in the structure of biological macromolecules.
The fundamental elements are hydrogen (H), carbon (C), nitrogen (N), and oxygen (O).
What is the significance of the outer shell in atomic structure?
The outer shell of an atom determines its chemical properties and reactivity.
Describe the change in the carboxyl group at physiological pH.
At most physiological pH, the carboxyl group (COOH) loses a hydrogen ion (H+) and becomes COO-.
How does the amino group change at physiological pH?
At most physiological pH, the amino group (-CNH2) gains a hydrogen ion (H+) and becomes -CNH3+.
Define zwitterion in the context of amino acids.
A zwitterion is a form of an amino acid that has no net charge, occurring at virtually all physiological pH.
Explain the significance of the alpha carbon in amino acids.
The alpha carbon (Cα) is tetrahedral and connected to four different groups, making it chiral and allowing the amino acid to exist as two enantiomers.
What are the two forms of amino acids based on chirality?
The two forms of amino acids based on chirality are L (Laevo) and D (Dextrorotatory) forms.
How can L and D amino acid isomers be interconverted?
L and D amino acid isomers can only be interconverted by breaking a chemical bond.
Identify the common occurrence of amino acids in proteins.
Only L-amino acids are found in proteins, except on very rare occasions.
What happens to the electron pairs in the carboxyl group during ionization?
The pair of electrons that formed the OH bond and one of the bonds in C=O become delocalized and are shared between the COO- group.
Describe the role of side chains in amino acids.
The side chains, labeled as R groups, determine the character of each of the twenty amino acids, influencing their properties such as acidity, basicity, hydrophobicity, and hydrophilicity.
Define essential amino acids.
Essential amino acids are those that humans cannot synthesize and must obtain from their diet. There are eight essential amino acids.
How many variations of amino acids exist and what differentiates them?
There are twenty variations of amino acids, differentiated by the side chains (R groups) attached to the central carbon atom.
List the essential amino acids.
The essential amino acids are Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan, and Valine.
What is the significance of the CORN law in amino acids?
The CORN law is a mnemonic used to determine the configuration of amino acids, indicating the arrangement of the amino group (C), the carboxyl group (O), the R group (R), and the hydrogen atom (N) around the central carbon.
Explain the difference between hydrophobic and hydrophilic amino acids.
Hydrophobic amino acids contain only carbon and hydrogen in their side chains, making them non-polar, while hydrophilic amino acids contain oxygen or nitrogen, making them polar and able to interact with water.
Identify the non-essential amino acids.
The non-essential amino acids are Alanine, Arginine, Asparagine, Aspartate, Cysteine, Glutamate, Glutamine, Glycine, Histidine, Proline, Serine, and Tyrosine.