Amino Acids Quiz

The basic building blocks of proteins and peptides.

Amino acids that cannot be synthesized by the body and must be obtained from the diet.

Short chains of amino acids.

Large, complex molecules composed of amino acids linked together by peptide bonds.

An amino acid that has both a positive and negative charge.

The non-variable part of an amino acid, consisting of a central carbon atom bonded to an amino group, a carboxyl group, and a hydrogen atom.

The variable part of an amino acid, that determines its unique properties.

The presence of six amino acids with aliphatic side chains, generally hydrophobic.

Aspartate, Glutamate, Asparagine, and Glutamine are amino acids with side chains that contain carboxyl groups or amides.

Arginine and Lysine have basic side chains, which contain either a guanidine or amine group.

Histidine, Tryptophan, Phenylalanine, and Tyrosine are amino acids with aromatic side chains. Histidine is weakly basic, while tyrosine is weakly acidic. Phenylalanine and Tryptophan are hydrophobic.', 'term': 'Aromatic Amino Acids', 'hint': 'Think of the 'H', 'W', 'F', and 'Y' - they're the aromatic amino acids.', 'memory_tip': 'Aromatic rings - they're like rings on a finger, but chemically they have a special smell!' }, {

Cysteine and Methionine are amino acids with side chains containing sulfur; Cysteine is a thiol, and Methionine is a thioether.

A process where DNA is used as a template to create a complementary RNA molecule.

A three-base sequence in mRNA that codes for a specific amino acid. For example, the codon UUC codes for phenylalanine.

The process of converting the genetic code from mRNA into a protein sequence.

Enzyme responsible for synthesizing RNA during transcription.

A molecule that carries amino acids to the ribosome during protein synthesis. It has an anticodon that recognizes a specific codon on mRNA.

A complex structure where translation takes place. It reads the mRNA codons and assembles the polypeptide chain.

The site where the next amino acid is added to the growing protein chain. The ribosome moves along the mRNA strand, reading each codon.

The site where the tRNA carrying the growing polypeptide chain is held.

A type of covalent bond formed between two cysteine amino acid residues, where the sulfur atoms of the side chains are linked by a disulfide bridge.

A molecule that binds to a protein, typically at a specific site called the binding site.

The linear sequence of amino acids in a protein, starting from the N-terminus and ending at the C-terminus.

The three-dimensional arrangement of a protein's polypeptide chain, formed by hydrogen bonds between backbone atoms.

A secondary structure where polypeptide chains align in an antiparallel fashion, with hydrogen bonds forming between backbone atoms.

A type of secondary structure formed by a helical arrangement of the polypeptide chain, stabilized by hydrogen bonds between backbone atoms.

The three-dimensional structure of a protein, formed by interactions between side chains of amino acids.

The overall three-dimensional structure formed by two or more polypeptide chains interacting.

A type of protein that is responsible for the structure and integrity of cells and tissues.

A protein that is involved in the processes of catalysis, transportation, and regulation within a cell.

Hydrophobic sidechains are found within the protein interior, driving protein folding and enabling proteins to span membranes, forming bridges or tunnels between different cellular compartments.

Glycine (Gly) and Proline (Pro) have unique structures that make them flexible and rigid respectively, often found at the ends of secondary structures and within hinge/loop regions.

In a typical cellular environment, acidic sidechains lose a proton (H+) and become negatively charged, while basic sidechains gain a proton (H+) and become positively charged.

Electrostatic interactions, formed by the attraction of opposite charges, occur between acidic and basic sidechains, contributing to protein stability and interactions.

Salt bridges, a type of electrostatic interaction, occur between charged sidechains of specific amino acids like Arginine (Arg) and Lysine (Lys).

Electrostatic interactions (+blue/-red) can be visualized in protein structures, highlighting how these interactions contribute to protein interactions and stability.

Proteins can interact with each other through electrostatic interactions. This is particularly important for protein-protein recognition events.

Electrostatic interactions play a vital role in protein structure and function, influencing protein folding, stability, and interactions with other molecules.