Macromolecules

Carbon Framework

Biological molecules primarily consist of carbon atoms bonded to hydrogen, oxygen, nitrogen, sulfur, or phosphorus.

Functional Groups

Attachments to a core carbon power unit that give molecules distinct chemical properties.

Hydroxyl Group ($- ext{OH}$)

Polar group found in carbohydrates, proteins, nucleic acids, and lipids.

Carbonyl Group ($- ext{C=O}$)

Polar group found in carbohydrates and nucleic acids.

Carboxyl Group ($- ext{COOH}$)

Acidic group found in proteins and lipids.

Amino Group ($- ext{NH}_2$)

Basic group found in proteins and nucleic acids.

Sulfhydryl Group ($- ext{S-H}$)

Group that forms disulfide links; found in proteins.

Phosphate Group ($- ext{PO}_4^{2-}$)

Charged group found in nucleic acids.

Methyl Group ($- ext{CH}_3$)

Nonpolar group found in proteins and nucleic acids.

Isomers

Molecules with the same molecular formula but different structures.

Structural Isomers

Isomers with identical groups bonded to different carbons.

Stereoisomers

Isomers with the same carbon backbone but differing in spatial group attachment.

Enantiomers

Non-superimposable mirror-image chiral molecules.

Dehydration Synthesis

Reaction where monomers assemble into polymers by removing $ ext{H}_2 ext{O}$.

Hydrolysis

Reaction where polymers break down into monomers by adding $ ext{H}_2 ext{O}$.

Monosaccharides

Single sugar units; energy source and structural components of nucleotides.

Disaccharides

Two monosaccharides joined via dehydration; examples include sucrose and lactose.

Storage Polysaccharides

Polysaccharides like starch and glycogen used for energy storage.

Structural Polysaccharides

Polysaccharides like cellulose and chitin providing structural support.

Nucleotide

Monomer of nucleic acids; consists of a 5-carbon sugar, phosphate group, and nitrogenous base.

Pyrimidines

Single-ring nitrogenous bases; include cytosine, thymine, and uracil.

Purines

Double-ring nitrogenous bases; include adenine and guanine.

Base Pairing

Adenine pairs with Thymine/Uracil, Cytosine pairs with Guanine.

DNA

Double-stranded helix with antiparallel strands; uses deoxyribose sugar.

RNA

Single-stranded, uses ribose sugar; includes mRNA, tRNA, and rRNA.

ATP

Adenosine Triphosphate; provides cellular energy when phosphate bonds break.

Proteins

Molecules with functions including enzyme catalysis, transport, and defense.

Amino Acids

Monomers of proteins linked via peptide bonds.

Primary Structure

Linear amino acid sequence of a protein.

Secondary Structure

Local folding into structures like $\beta$-pleated sheets; stabilized by hydrogen bonds.

Tertiary Structure

Overall 3D shape of a protein driven by various interactions.

Quaternary Structure

Complex formed by multiple polypeptide chains.

Motifs

Common folding patterns in proteins.

Domains

Functional units in proteins that perform specific tasks.

Chaperone Proteins

Proteins that assist in proper folding and refolding of other proteins.

Triglycerides

Lipid made of 1 glycerol and 3 fatty acid chains.

Saturated Fatty Acids

Fatty acids with no double bonds, resulting in straight chains.

Unsaturated Fatty Acids

Fatty acids containing double bonds, resulting in kinks.

Phospholipids

Lipids made of a glycerol backbone, 2 fatty acids, and a phosphate group.

Cell Membranes

Formed by phospholipids creating lipid bilayers or micelles.

Other Lipids

Includes steroids, terpenes, prostaglandins, waxes, and carotenoids.

Distinctive characteristics exclusive to DNA

Double-stranded helical molecule containing deoxyribose sugar and the nitrogenous base thymine.

Distinctive characteristics exclusive to RNA

Typically single-stranded molecule containing ribose sugar, the nitrogenous base uracil, and functioning in forms such as mRNA, tRNA, and rRNA.

Shared structural components of both DNA and RNA

Nucleic acid polymers made of nucleotide monomers, each containing a 5-carbon sugar, a phosphate group, and the nitrogenous bases adenine, guanine, and cytosine.

DNA

A–T, C–G

RNA

RNA: A–U, C–G

Functional order in protein synthesis

DNA mRNA, rRNA, tRNA.

mRNA

Messanger, carries genetic info

tRNA

carries amino acid

rRNA

part of the ribosome

denaturation

protein unfolded or changes shape

why does denaturation happen

pH, temp, and concetration change

dissosication

Happens in quatiatery structure, subunits may be seperated w/o loosing tertiary structure

renaturation

proteins enviroment back to normal, may be refolded

L amino acids

found in proteins

What makes an amino acid chiral?

Central carbon bonded to 4 different groups (glycine does not do this so not chiral)

structure of amino acid

Carboxyl froup, amino group, R group, Hydrogen, central carbon