unit 2 - molecular bio

water molecule

polar, universal solvent

covalent bond

sharing of electrons

hydrogen bond

strongest IMF, weaker than ionic and covalent bonds

cohesive properties

attraction between water molecules, makes surface tension

adhesive properties

attraction between water and other polar molecules, adheres to cellulose in xylem

solvent

able to dissolve other substances

hydrophilic

water loving

hydrophobic

water fearing, insoluble in water

thermal properties

high specific heat capacity → raising temp with energy

water Cs

high because h-bonds → restrict motion

high latent heat of vaporization

energy to separate liquid molecules to become vapour

NaCl

ionic, carried in blood plasma

glucose

polar, transported in blood plasma, used in aerobic respiration

oxygen

non-polar, too small to dissolve in water → carried in RBCs/red blood cells

amino acids

negative/positive charge, soluble + carried in plasma

cholesterol

hydrophobic + insoluble in water

fats

non-polar + insoluble in water

methane

non-polar, with super low boiling+melting point

water vs. methane

water has H-bonds and is polar so it allows it to have higher heat capacity and boiling points than methane

where fats and cholesterol are transported in

in the lipoprotein complex (phospholipid sphere)

metabolism

all enzyme catalyzed reactions in our body

factors of chem. reactions

molecules that are colliding, orientation of them, speed of collision

major macromolecules

polymers

monomers

building blocks/ sub components of polymers

anabolism

building large molecules - need energy, releases water

catabolism

break apart large molecules - releases energy, need water (hydrolysis reaction)

enzymes

proteins that can help reactions occur faster without being used in reaction, lower activation energy

urea (CO (NH2)2)

disproved vitalism

vitalism

organic molecules can only be made by living things

monosaccharide

single sub-unit sugars, 1:2:1 ration of CHO

ex of monosaccharide

glucose, ribose, galactose, fructose

disaccharide

two monosaccharides, have double ring structure

ex of disaccharides

sucrose, lactose, maltose

polysaccharide

starch, glycogen, cellulose

fructose

fruit sugar (mono)

galactose

nutritive sweetener (mono)

maltose

malt sugar in barley (di)

lactose

sugar in milk (di)

sucrose

transport sugar found in plants (di)

starch

store carbohydrates in plants (poly)

cellulose

build cell walls (poly)

glycogen

store carbohydrates in animals (poly)

amylase

enzyme that breaks starch → maltose

glycogen phophorylase

enzyme that breaks glycogen into glucoses

glycosidic bond

bond between carbohydrates (has O between)

iodine

used to detect starches

benedict’s solution

used to detect simple sugars

successful chemical reactions depend on

molecules colliding, orientation and the collision speed (temp can affect)

amylose

linear starch

amylopectin

branched starch

steroid

lipids that are hormones

tryglyceride

lipids used for storage

phospholipid

lipids used in membrane (2 f.a. and phosphate group to a glycerol)

glycerol

liquid compound, is a solvent and sweetener, used to make soaps and lotions

adipose tissue

connective tissue under the skin made of lipids

cis fats

naturally occuring, bent chain and are liquid at room temp

trans fats

man-made, straight chain, solid at room temp

body mass index

mass (kg) / height 2 (m)

polypeptide

chain of a.a.

primary structure

chain of ribosomes (peptide bonds)

secondary structure

alpha helix/ beta sheets (H bond interactions)

tertiary structure

globular protein (R group interactions)

quaternary structure

active protein (2+ polpeptides)

proteome

all the proteins in a genome

insulin

globular protein that is produced by beta cells in pancreas (uptake of glucose in blood)

immunoglobulins

globular protein that fights infections by recognizing and binding to antigens

rhodopsin

globular protein that is a pigment in photoreceptor cells in retina (allows low light intensities to be detected)

collagen

fibrous protein in muscles, tendons and ligaments, provides tensile strength to prevent tearing

substrate

substance that turns into product

active site

area for substrate binding

temperature

high temp speed up particles = more ke = more collisions

pH

optimal ph = best for enzymes to work

substrate concentration

higher concentration = more active sites filled = faster reaction rate

denature

structural change in a protein making it lose its function/ biological properties

immobilized enzyme

mobility immobilized in a calcium alginate gel, enzyme aggregates, or attached to another material like glass

activation energy

energy needed to overcome for chemical reaction to occur

competitive inhibitor

molecule with similar shape sits in active site , reversible

non-competitive inhibitor

molecule binding to enzyme away from active site, reversible

allosteric site

site that allows molecules to activate/inhibit enzyme activity

end-product inhibition

prevents cell from making more of smt when have suff. amt (negative feedback loop)

antimalarial drugs

hydrophobic protein

r groups on inside of protein

hydrophillic protein

r groups on outside of protein

rubisco

globular enzyme involved in fixation of CO2 in chloroplasts

spider silk

fibrous protein that can be extended and resistant to breaking

binding site

part of active site, binds and orientates substrates

catalytic site

part of active site, lowers activation energy

why immobilize enzymes

convenience (can stop rxn at any time), economics (enzyme can be recycled and reused), stability ( more temp and ph stable), higher rxn rate

lactose free milk

break lactose down (galactose and glucose) less sugar needed in sweet foods, faster production of yogurt and cottage cheese