The Chemical Level of Organization Flashcards

Vocabulary flashcards covering key chemical concepts, atomic models, functional groups, biological macromolecules, protein structures, enzyme mechanisms, and nucleic acids from the lecture notes.

Chemistry

The science of the structure and interactions of matter.

Matter

Anything that occupies space and has mass.

Mass

The amount of matter in any object, which does not change.

Weight

The force of gravity acting on matter, which does change.

Free Radical

An atom or group of atoms with an unpaired electron in the outermost shell, making it unstable, highly reactive, and destructive to nearby molecules.

Atomic Number

The number of protons in an atom.

Mass Number

The total number of protons and neutrons in an atom.

Atomic Mass

The average mass of all stable atoms of a given element in daltons.

Electron Cloud Model

A model of atomic structure where the shading represents the chance of finding an electron in regions outside the nucleus.

Electron Shell Model

A model of atomic structure where filled circles represent individual electrons grouped into concentric circles according to their shells.

Hydroxyl Group

An $-OH$ group found in alcohols that is polar and hydrophilic due to its electronegative oxygen atom.

Sulfhydryl Group

An $-SH$ group found in thiols that is polar and hydrophilic, helping to stabilize protein shape in amino acids like cysteine.

Carbonyl Group

A polar and hydrophilic group consisting of a carbon atom double-bonded to an oxygen atom, found within carbon skeletons in ketones and at the end in aldehydes.

Carboxyl Group

A $-COOH$ group found at the end of carboxylic acids and all amino acids, whose negatively charged form predominates at cellular pH.

Ester Group

A functional group that $\text{predominates}$ in dietary fats and oils as triglycerides, and occurs in aspirin as an ester of salicylic acid.

Phosphate Group

A $-PO_4^{2-}$ group that is very hydrophilic due to its dual negative charges, crucial for transferring chemical energy in ATP.

Amino Group

An $-NH_2$ group found at one end of all amino acids that acts as a base by picking up a hydrogen ion to carry a charge of $1^+$ at body fluid pH.

Functional Groups Table

A structural reference table outlining key organic functional groups including Hydroxyl, Sulfhydryl, Carbonyl, Carboxyl, Ester, Phosphate, and Amino groups.

Monosaccharides

Simple sugars containing $3$ to $7$ carbon atoms, such as glucose, fructose, galactose, deoxyribose, and ribose.

Disaccharides

Carbohydrates formed from the dehydration synthesis of two monosaccharides, such as sucrose, lactose, and maltose.

Polysaccharides

Carbohydrates containing tens to hundreds of monosaccharides joined by dehydration synthesis, such as glycogen, starch, and cellulose.

Lipoproteins

Soluble lipid-protein complexes that transport lipids in blood plasma by surrounding inner hydrophobic lipids with outer hydrophilic proteins.

Saturated Fatty Acid

A fatty acid containing only single covalent bonds between carbon atoms in its hydrocarbon chain.

Unsaturated Fatty Acid

A fatty acid containing one or more double covalent bonds between carbon atoms, producing a kink at each double bond.

Primary Structure

The genetically determined, unique one-dimensional linear sequence of amino acids linked by peptide bonds.

Secondary Structure

The repeated twisting or folding of neighboring amino acids in a polypeptide chain, forming alpha helixes or beta pleated sheets stabilized by hydrogen bonds.

Tertiary Structure

The three-dimensional folding pattern of a polypeptide chain that determines its specific biological function.

Quaternary Structure

The three-dimensional arrangement resulting from the combination of two or more individual polypeptide chains.

Fibrous Proteins

Water-insoluble proteins with parallel strand structures that serve structural roles, including collagen, elastin, keratin, dystrophin, fibrin, actin, and myosin.

Globular Proteins

Water-soluble, spherical proteins that perform metabolic functions, including enzymes, antibodies, hemoglobin, albumins, and insulin.

Denaturation

The process by which a protein unravels and loses its characteristic three-dimensional shape in an altered environment, rendering it non-functional.

Apoenzyme

The protein portion of an enzyme molecule that requires a cofactor to become active.

Cofactor

The non-protein component of an enzyme, which may be a metal ion (such as $Fe$, $Mg$, $Zn$, or $Ca$) or an organic coenzyme.

Coenzyme

An organic molecule, often derived from vitamins, that acts as a non-protein cofactor for an enzyme.

Mechanism of Enzyme Action

The three-step catalytic pathway where substrates bind to the active site to form an enzyme-substrate complex, undergo transformation into products, and leave the enzyme unchanged to repeat the cycle.

Deoxyribonucleic Acid (DNA)

A double-stranded helical nucleic acid containing deoxyribose sugar and bases adenine, thymine, cytosine, and guanine that stores inherited genetic material.

Ribonucleic Acid (RNA)

A single-stranded nucleic acid containing ribose sugar and bases adenine, uracil, cytosine, and guanine that relays genetic instructions to guide protein synthesis.

Purines

Larger, double-ring nitrogenous bases comprising adenine and guanine.

Pyrimidines

Smaller, single-ring nitrogenous bases comprising thymine, cytosine, and uracil.

Adenosine Triphosphate (ATP)

A high-energy molecule consisting of three phosphate groups attached to adenosine that transfers energy liberated from catabolic reactions to power cellular work.