Chapter 2: Basic Chemistry Flashcards
major essential elements
carbon, hydrogen, oxygen
molecule
2 or more atoms sharing electrons
isotopes
different mass, same protons
non-polar covalent bond
electrons shared equally between atoms, no net charge
polar covalent bond
one atom has stronger pull on electrons, H2O, oxygen has more protons, pulls electrons, gets negative charge
hydrogen bond
opposite charges of polar molecules attract, holds water together and dna strands
NH2
COOH
OH
H2PO4
amino
carboxyl
hydroxyl
phosphate
4 categories of biomolecules
carbohydrates
lipids
proteins
nucleotides
carbohydrates
- formula
- monomer (ex)
- polymer (ex)
most abundant
- CH2O
- monosaccharides (gluose, ribose)
- polysaccharides (glycogen, starch)
polysaccharide storage
liver and muscle
breakdown of disaccharides
- sucrose
- maltose
- lactose
- sucrose = glucose + fructose
- maltose = 2 glucose
- lactose = glucose + galactose
lipids
- make up
- monomer
- polymers
- carbons and hydrogens, few oxygens
- fatty acid (saturated or unsaturated)
- triglycerides, phospholipids, steroids
saturated vs unsaturated fatty acids
saturated: no double bonds, bad
unsaturated: 1 or more double bonds, saturated with H+s
triglycerides makeup
glycerol + 3 fatty acids
phospholipid makeup
phosphate + 2 fatty acids
eicosanoid makeup
C ring + 2 long carbon chain tails
steroid makeup
4 linked rings (cholesterol)
nucleotides
- makeup
- composition
- monomer
- polymer
- function
- N, C, H, O
- base, sugar, phosphate
- nucleotide
- nucleic acids
- transmit and store information, transfer energy, store energy, messanger
how bases pair
G=-C, A=T, A=U in RNA
proteins
- makeup
- monomer
- polymer
- levels of organization
- C, H, O, N
- amino acids
- polypeptide/protein
- primary, secondary, tertiary, quarternary
protein structure
C attached to H, COOH, R, NH2 (clockwise from top)
peptide bond
COOH + NH2 = OC-NH (released H2O)
secondary structure
alpha helix, beta pleated sheets
tertiary structure
globular -soluble in water -carriers, enzymes, hormones, neurotransmitters -alpha helix primary fibrous -insoluble in water -collagen, keratin
quarternary structure
2+ tertiary subunits
fibrous -> collagen
globular -> hemoglobin
acids vs bases
acids: give off H+
bases: take H+
pH formula
pH = log (1/[H+])
pH of blood
7.4, basic
enzymes
catalyze chemical reactions
membrane transporters
move substance across cell membranes
signal molecules
communicators between cells of body, typically bind to proteins at the receiving end
hormones, neuropeptides
receptors
bind signal molecules, precipitate action within cell
binding proteins
bind and transport molecules (hemoglobin), protein chaperones, mostly in ECF
immunoglobins
antibodies, immune response,
regulatory proteins
transcription factors, regulation of gene expression
ligand
molecule that binds to a protein
induced-fit model
protein changes shape to better fit ligand
proteolytic activator
removes peptide fragments from inactive protein to make it active
allosteric activator
binds away from binding site, activates protein
cofactors
bind to binding site to make it active
competitive inhibitor
binds to binding site, blocks ligand
allosteric inhibitor
binds away from binding site, inactivates protein
covalent modulator
binds to protein and changes its activity
agonist
synergist, works together
antagonist
opposites, works against
protein concentration factor
ever increasing
ligand concentration factor
increases to a point, then levels out at saturation point
buffer
minimizes changes of pH, takes excess H+ out of solution or contributes when running out
bicarbonate in blood
