Unit 1: Chemistry of Life Flashcards
Chemistry of Life
Hydrophobic vs Hydrophilic
Phobic: hates water and repels away (ex. non-polar tails in membrane)
Phillic: love water and is attracted to it (polar things)
Cohesion vs Adhesion
Cohesion: water attracted to water (cohesion = co/ same ting working together)
Adhesion: water attracted to other polar things
Surface tension and capillary action are examples of cohesion + adhesion
Capillary Action
The combination of adhesion and cohesion inside a plant
Universal Solvant
water (effectively dissolves any polar/ionic substance)
water itself is a polar molecule
Carbohydrate
elements: carbon, oxygen, and hydrogen (makes a hexagon shape)
monomer: monosaccharides (polysaccharides is multiple)
functions: ENERGY (glucose) and structural support (ex. cellulose)
Protein
elements: carbon, oxygen, hydrogen, nitrogen, and SULFUR
monomers: amino acids (form peptide chains and have four states of protein conformation) - amino acids are bonded together with covalent bonds
functions: messengers, structure, transportation, defense, and ENZYMES
Nucleic Acid
elements: carbon, hydrogen, oxygen, nitrogen, and PHOSPOROUS
monomer: nucleotides - phosphate + sugar (ribose or deoxyribose) + nitrogenous base (A, T, G, C, or U)
functions: store and transfer genetic information as DNA or RNA (high energy)
Lipids
elements: carbon, hydrogen, oxygen, (can sometimes have phosphorus)
NONPOLAR (like tails in membrane)
monomer: depends on lipid, triglycerides, steroids, or phospholipids
functions: long term energy storage, insulation, floatation, hormones, cell membrane
Dimer
two monomers put together
Hydrolysis
uses water to break down COVALENT bonds between compounds
used for breaking down macromolecules
Dehydration Synthesis
how cells build polymers and other things (water is removed and a covalent bond is formed)
synthesis = creation (water is a product of this reaction)
Peptide Bond
covalent bond between two amino acids (peptide and polypeptides are both proteins)
4 stages of protein conformation
amino acids are made up of NH3, COO, and an r-group, the r-group is the only thing that changes to determine how the protein will fold
Primary: amino acids bond together to form a string of amino acids (like beads on a string
Secondary: amino acid r- group interactions create a Alpha Helix or a beta sheet structure
Tertiary: single fully folded polypeptide
Quaternary: tertiary structures combine (ex. hemoglobin) - not all proteins do this, some stop at tertiary, but if protein are supposed to do this and don’t then that protein is considered damaged
Protein Denature
when a protein misfolds to the wrong shape in certain Enviromental conditions
- high temps (too much heat can break bonds)
- extreme ph (acid or base and cause denature)
DNA vs RNA
DNA: Deoxyribonucleic acid
- bases: A + T, C + G
- mostly two strands (can be one)
-deoxy = missing oxygen atom
RNA: Ribonucleic acid
- bases: A + U, G + C
- mostly one strand (can be two)
BOTH:
- run antiparallel with 5 prime end (phosphorous exposed) and 3 prime end (exposed sugar/ OH)
- nitrogenous bases bond with hydrogen bonds
- both Deoxyribose and Ribose are PENTOSE sugars (5 carbons)
Chargaff’s Rule
DNA: A always pairs with T, C always pairs with G
RNA: A always pairs with U, C always pairs with G
