Basis of Life Flashcards
(22 cards)
Metabolism
Sum of all chemical reactions that occur in the body
Catabolic: break down large chemicals and release energy
Anabolic: build up large chemicals and require energy
Ingestion
Acquisition of food and other raw materials
Digestion
Process of converting food into a soluble form so it can pass through membranes in digestive tract
Absorption
Passage of nutrient molecuels through lining of digestive tarct into body via diffusion/active transport
Transport
Circulation of essential compounds required to nourish the tissues and removal of waste products from tissue
Assimilation
Building up new tissues from digested food materials
Respiration
Consumption of oxygen by body. Oxygen is needed to convert glucose –> ATP (ready energy source for cellular activities)
Excretion
Removal of waste products
Synthesis
Creation of complex molecules from simple areas (anabolism)
Regulation
Control of physiological activities to achieve homeostasis
Irritability
Ability to respond to a stimulus
Photosynthesis
plants convert CO2 and H2O into carbohydrates.
Sunlight is harnessed via chlorophyll driven reaction
Protoplasm
Substance of life
Primary- C,H, O, N, S, P
Traces of- Mg, I, Fe, Ca and other materials
Inorganic compounds
Compounds without Carbon (salts and HCl)
Organic compounds
Compounds made by living systems; contain Carbon
(carbohydrates, lipids, proteins, nuleic acids)
Carbohydrates
C, H, O
1:2:1 ratio
Storage forms of energy (glucose/glycogen in animals)
Strucutral molecules (starch in plants)
Monosaccharide: single sugar subunit (glucose, fructose)
Disaccharide: 2 monosaccharide subunits joined by dehydation synthesis (loss of H20) : maltose and sucrose
Polysaccharide: polymers (multiple monosaccharides) - (glycogen, starch, cellulose)
Dehydration reaction ( remove H20)
Adding h20 (hydrolysis) breaks down polymers
Lipids
(fats/oils)
composed of C,H and O; H:O ratio is high
triglyceride: lipid w/ 3 fatty acids bonded to a glycerol backbone
fatty acid- long carbon chains- gives hydrophobic characteristic. and carboxylic acid groups- makes acidic
3 dehydration reactions = 1 fat molecule
don’t form polymers
food storage in animals
heaviest “compound”
insulation/protection (fatty tissue - adipose)
Phospholipid: glycerol, 2 fatty acids, phosphate groups, Nitrogen w/ alcohol
lecithin: cell membrane
cephatin: brain, nerves, neural tissue
Waxes: esters of fatty acids + monohydroxylic alcohol. Protective coating on skin, fur, leaves, exoskeltons
Steriods: 3 fused cyclohexane rings and one fused cyclopentane ring. (Cholesterol, testosterone, estrogen, corticosteroicls)
Caroteroids: fatty, acid like carbon chains containing double bonds, 6 carbon rings. Pigments producing red orange yellow and brown colors in animals/plants
Porphyrins (tetrapyrroles): 4 joined pyrrole rings - metal
Proteins
C, H, O, N ( P & S)
polymers of amino acids
amino acids joined by peptide bonds (dehydration rxns)
polypeptide: chains of peptide bonds. peptide=polymer
primary strucutre: sequence of amino acids in protein
secondary strucutre: hydroen bonding between adjacent amino acids. can coil/fold to form alpha helices and beta pleated sheets (part of secondary strucutre)
tertiary: 3D strucutre; K group interactions between adjacanet amino acids (globular/fibrous proteins)
quaternary: interaction and joining of 2+ independent polypeptide chains
Protein classifications by strucutre:
simple: compound with all amino acids
albuming/globuling: primarliy globular in nature. functional proteins act as carriers or enzymes
scleroproteins: fibrous in nature and act as strucutral proteins (collagen)
conjugated: simple protein plus one non protein fraction
lipportein: protein+ lipid
glycoprotin: protein + carb
chromoprotein: protein + pigmented molecules
metallproteins: proteins around a metal ion
nucleprotein: protein containing histone or protamine (juclear protein) bound to nucleic acids
Functions of Proteins
hormones: chemical messengers (insulin, ACTH)
enzymes: catalys, increase rate of reaction (amylase, lipase, ATPase)
strucutral proteins physical support of tissues/cells. Extracellular: collagen in bone/cartilage/tendon Intracellular: proteins in cell membrane
Transport: carriers of importatin materials (hemoglobin (O2 in blood) and cytochromes (carry electron in cellular respiration)
antibodies: bind to foreing particles (antigens)- disease causing organisms
Enzymes
*dont alter equilibrium constant
*not consumed in reaction: found in products/reactants
*pH/ temperature sensitive
- organic catalysts (increase rate of rxn w/out changing itself)
regulate metabolism- lower activation energy
proteins can form 1000s of enzymes (conjugated proteins with non protein enzyme)
very selective
substarte: molecule enzyme acts on
active site: area on enzme where substate binds
binding: lock and key & induced fit
reversable reactions
temperature sensitive, increase in temp = increase rate of reaction
ph sensitive- good around 7
except pepsin (ph=2)
pancreatic enzymes (ph 8.5)
competitive inhibition: substrates compete for active site
noncompetitive inhibition: oppisite.
allosteric inhibition: inhibition not @ active site
hydrolysis: adding h20 to break down polymers
lactase hydrolyzes lactose to glucose and galactose
proleases degrade proteins to amino acids
lipases break down lipids to fatty acids and glycerol
synethesis (dehydrations- losing h20, forms polymers)
catalyzed by same enzymes just reverse reactions
cofactors: non protein molecule makes enzymes active- metal cations (zn fe) or small organic groups
Cell Strucutre
Strucutre- function
organelles: nucleus, ribosome, endoplasmic reticulum, golgi aparatus, vesicles, vacuoles, lysosomes, itchondria, chlorplasts, centrioles
