BIO 1203 Chapters 1-5 Flashcards

Comprehensive vocabulary flashcards covering basic chemical concepts, water properties, carbon chemistry, macromolecules, and biological themes from Chapters 1 through 5.

Trace elements

Elements required by organisms in minute amounts, such as Fe, I, and Zn.

Isotopes

Atoms of the same element with the same number of protons but a different number of neutrons, such as $^{14}\text{C}$ used for dating and tracing.

Nonpolar covalent bond

A covalent bond in which electrons are shared equally between atoms, such as $\text{H–H}$.

Polar covalent bond

A covalent bond in which electrons are shared unequally, such as in $\text{H}_2\text{O}$ where oxygen pulls electrons more strongly.

Ionic bond

A chemical bond resulting from the transfer of electrons, forming ions such as $\text{Na}^+$ and $\text{Cl}^-$.

Hydrogen bond

A weak chemical bond where a hydrogen atom is attracted to an electronegative atom like oxygen (O) or nitrogen (N).

Chemical equilibrium

The state in a chemical reaction where forward and reverse reaction rates are equal, which does not mean concentrations are equal.

Cohesion

The property of water molecules sticking to other water molecules.

Adhesion

The property of water molecules sticking to other surfaces.

Hydrophilic

Water-loving substances that are polar or charged.

Hydrophobic

Water-fearing substances that are nonpolar, such as oils.

pH scale

A logarithmic measure of hydrogen ion concentration defined by $\text{pH} = -\log[\text{H}^+]$, where values below 7 are acidic, above 7 are basic, and equal to 7 are neutral.

Buffers

Substances such as bicarbonate that resist pH changes by absorbing or releasing $\text{H}^+$.

Evaporative cooling

Cooling caused by heat of vaporization during phase change, seen in sweating or panting.

Hydrocarbons

Molecules composed only of carbon and hydrogen that are hydrophobic and store high energy.

Structural isomers

Isomers that differ in the covalent arrangements of their atoms.

Geometric isomers

Isomers that have the same covalent bonds but differ in spatial arrangement (cis/trans).

Enantiomers

Isomers that are mirror images of each other, which are important in pharmaceutical drugs.

ATP (Adenosine Triphosphate)

A molecule consisting of adenosine bonded to 3 phosphate groups that releases cellular energy via hydrolysis to ADP.

Dehydration reaction

A chemical reaction that builds polymers by removing a water molecule ($\text{H}_2\text{O}$).

Hydrolysis

A chemical reaction that breaks polymers into monomers by adding a water molecule ($\text{H}_2\text{O}$).

Glycosidic linkage

The covalent bond that joins monosaccharide units to form carbohydrates.

Ester linkage

The bond formed between glycerol and fatty acids in lipids.

Peptide bond

The covalent bond linking amino acids together in a polypeptide chain.

Phosphodiester bond

The covalent bond connecting nucleotides in nucleic acids like DNA and RNA.

Starch

A helical storage polysaccharide in plants made of $\alpha$ glucose monomers that can be digested by humans.

Cellulose

A straight structural polysaccharide in plants made of $\beta$ glucose monomers that acts as fiber and cannot be digested by humans.

Saturated fats

Fats with no double bonds that are solid at room temperature and typically derived from animal sources.

Unsaturated fats

Fats containing double bonds that are liquid at room temperature and typically derived from plant or fish sources.

Phospholipids

Lipids consisting of a hydrophilic head and hydrophobic tails that form the cell membrane bilayer.

Steroids

Lipids characterized by a carbon skeleton composed of 4 fused rings, such as cholesterol, estradiol, and testosterone.

Primary structure of protein

The unique sequence of amino acids in a polypeptide chain.

Secondary structure of protein

Coils and folds ($\alpha$-helix or $\beta$-pleated sheet) in a polypeptide chain formed by hydrogen bonds in the backbone.

Tertiary structure of protein

The overall 3D shape of a protein resulting from interactions between R-groups (hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges).

Quaternary structure of protein

The protein structure resulting from the aggregation of multiple polypeptide subunits, such as in hemoglobin.

Denaturation

The process in which a protein unfolds and loses its biological function due to heat, pH, salt, or chemicals.

Gene expression

The process by which genetic information flows from DNA to RNA to Protein ($\text{DNA} \rightarrow \text{RNA} \rightarrow \text{Protein}$).

Negative feedback

A biological feedback mechanism in which the output opposes or reduces the initial stimulus (e.g., body temperature regulation).

Positive feedback

A biological feedback mechanism in which the output reinforces or amplifies the initial stimulus (e.g., childbirth).

Evolution

Descent with modification, where natural selection allows individuals with favorable traits to survive, reproduce, and adapt.