Nucleic Acids and Proteins Practice Flashcards

Vocabulary flashcards covering DNA, RNA, nucleotide structure, ATP energy reactions, protein structures, and hemoglobin based on lecture slides.

DNA (Deoxyribose Nucleic Acid)

A nucleic acid that stores genetic information, localized in the nucleus, consisting of deoxyribose sugar, a double helix structure, and nitrogenous bases Adenine, Guanine, Thymine, and Cytosine.

RNA (Ribonucleic Acid)

A single-stranded nucleic acid involved in protein synthesis, located throughout the cell, consisting of ribose sugar and nitrogenous bases Adenine, Guanine, Uracil, and Cytosine.

Nucleotide

The structural building block of nucleic acids composed of a sugar molecule, a phosphate group, and a nitrogenous base.

Pyrimidines

Single-ring nitrogenous bases that include Cytosine, Thymine, and Uracil.

Purines

Double-ring nitrogenous bases that include Adenine and Guanine.

Complementary Base Pairing

The specific hydrogen bonding between nitrogenous bases where Adenine pairs with Thymine (or Uracil in RNA) and Cytosine pairs with Guanine.

Adenosine Triphosphate (ATP)

The energy molecule of the cell consisting of adenine, ribose, and three phosphate groups, where the bond between the last two phosphate groups is high energy.

ATP Hydrolysis

An energy-releasing reaction represented by $\text{ATP} \rightarrow \text{ADP} + \text{P} + \text{energy}$, where breaking the high-energy terminal phosphate bond releases a large amount of energy.

Energy Hierarchy of Adenosine Phosphates

The energy relationship among cellular adenosine phosphates where the energy of $\text{ATP}$ is greater than the energy of $\text{ADP}$, which is greater than the energy of $\text{AMP}$.

Functional Proteins

Proteins that execute specific cellular tasks, including enzymes (reaction catalysts), antibodies (immune response), hormones (chemical messengers), and transport proteins such as hemoglobin.

Structural Proteins

Proteins that provide cellular support, such as keratin in fingernails and hair, and collagen in connective tissue.

Amino Acid Structure

A biological molecule containing a central carbon atom bonded to an amino group, a carboxyl group, and an R-side chain with $21$ possibilities that determine its biological properties.

Peptide Bond

A bond formed between two amino acids through a dehydration (condensation) reaction that removes a molecule of water.

Polypeptide

A polymer of amino acid monomers linked by peptide bonds, classified as a protein when it contains more than $50$ amino acids.

Primary Structure

The linear sequence of amino acids linked together in a polypeptide chain.

Secondary Structure

The spatial folding of a polypeptide chain into an $\beta$-pleated sheet or $\text{helix}$ stabilized by hydrogen bonds between the hydrogen of one amino acid and the oxygen of another.

Tertiary Structure

The overall three-dimensional shape formed by the folding of secondary structures of a polypeptide.

Quaternary Structure

The structural assembly formed when $2$ or more polypeptide chains combine together.

Hemoglobin

A quaternary transport protein found in red blood cells responsible for oxygen transport for respiration, composed of $4$ polypeptide chains ($2$ \text{\textalpha} subunits with $141$ amino acids and $2$ \text{\textbeta} subunits with $146$ amino acids) and iron (II)-containing heme groups.

Denaturation

The breaking of chemical bonds in a protein—often caused by heat, acids, or enzymes—which alters its shape and breaks its functional capacity.

Protein Folding Diseases

Pathological conditions arising when protein folding fails, such as CJD (Classic Creutzfeldt-Jakob Disease), vCJD (Variant Creutzfeldt-Jakob Disease), BSE (Bovine Spongiform Encephalopathy), and CWD (Chronic Wasting Disease).