anatomy exam 1 part 2

tonicity

solution’s ability to change the shape of the cell

lyse

burst

crenate

shrink

organic

contains carbon

why carbon?

electroneutral (4E in valence shell), small, abundant, can make long stable chains, more carbon = less likely to be polar

each carbon will form 4 ___ bonds

covalent

organic molecules

carbohydrates, proteins, lipids, nucleic acids

carbohydrates

contain carbon and H20 (“hydrated carbon”)

monosaccharides

1 carbon ring

monosaccharides examples

glucose, fructose, galactose

disaccharides

2 carbon rings

polysaccha

polysaccharides examples

starches, glycogen, cellulose

where is glucose found?

blood

carbohydrates are all ___ in water

soluble

very typical sugars

disaccharides

early soft drinks were mostly ___

sucrose

soft drinks now are ___

high fructose corn syrup

stored form of glucose

glycogen

where is glucose stored?

liver and muscle

why is cellulose important in the body?

plant cell walls, fiber, osmotic pressure pulls water into digestive tract

lipids

insoluble molecules made of carbon, hydrogen, oxygen

lipids have (higher/lower) oxygen than carbohydrates

lower

some lipids contain

phosphorous

triglycerides

neutral fats made of fatty acids and glycerol

triglycerides function s

energy storage, insulation, cushion

saturated triglycerides

single covalent bonds between carbons, solid at room temp, butter, animal fat

unsaturated triglycerides

1(mono-unsaturated) or more double(poly) covalent bonds , liquid at room temp, oil, plant fats

what are saturated fats “saturated” with?

hydrogen

phospholipids

modified triglycerides

phospholipid tail

nonpolar, 2 fatty acids, hydrophobic

phospholipid middle

1 glycerol

phospholipid head

polar phosphorous, hydrophilic

cholesterol

multi-carbon ring lipid

what makes cholesterol unique?

multi-carbon ring

cholesterol is important for

cell membranes, steroid hormones, bile salts

nucleic acids

largest molecule in the body, contains carbon, oxygen, hydrogen, phosphorous

2 classes of nucleic acids

deoxyribonucleic acids and ribonucleic acids

nucleotides

complex building blocks of DNA/RNA/ATP

in DNA and RNA, nucleotides are bound together by ___ bonds

covalent

nucleotides contain

sugar backbone, functional base, phosphate backbone

where is DNA found?

nucleus

DNA unique base

thymine

DNA function

to pull apart when needed

where is RNA found?

all over

RNA unique base?

uracil

RNA functions

temporary blueprint for making proteins, carries out order for protein synthesis

how many ATP molecules does a cell have?

1 billion

the ATP in a cell can last for ___ at rest

3 minutes

proteins

made of amino acids, held together by peptide (covalent) bonds, AA chains fold and form specific shapes dictated by the order of AAs

protein shapes are maintained by ___ and ___ bonds

hydrogen, covalent

denaturing affects mostly the ___ bonds

hydrogen

proteins make up ___% of cell mass

10-30

proteins all contain

carbon, hydrogen, oxygen, nitrogen (may have sulfur)

adults resynthesize ___% of their body protein every day

2-3

what is arguably the most important organic molecule

protein

why is protein the most important organic molecule

all body functions depend on it, proteins manufacture all other organic molecules

how many amino acids and what are their characteristics?

20, central carbon, carboxyl/organic acid group (COOH), amine/amino (basic) group (NH2), side group (R)

all amino acids are identical except for

the R group

R group importance

dictates characteristics of AA such as charge, pH, polarity, how it fits with other AAs

primary structure

determined by genetic instructions, AAs combine via dehydration synthesis

dehydration synthesis

acidic group bonds with basic group, loses water, forms a peptide bond

what type of bond is a peptide bond?

covalent

is dehydration synthesis an anabolic or catabolic reaction?

anabolic

secondary structure

alpha helix or beta sheet, determined by H bonds between R groups

tertiary structure

alpha helix/beta sheets fold on each other to form a globe/rope like structure, covalent & H bonds between R groups, R groups interacting with water

quaternary structure

2 or more peptides, not all proteins have quaternary structure

all structures arise due to

amino acid properties, amino acid relative location

denaturation

occurs due to loss of 2/3/4 structure, loses function due to shape change

causes of denaturation

pH, heat, toxic chemicals, radiation

protein types

fibrous, globular

fibrous protein

long/ropelike, insoluble, very stable, mainly structural proteins (collagen, myosin, cytoskeleton)

globular protein

compact/ball-like, soluble, chemically active (unstable) (hemoglobin, actin, enzymes, cell receptors, hormones, antibodies)

catalyst

increase rate of rxn by decreasing activation energy, shaped to fit reactants, charge of the pocket must work, ends with -ase

fluid mosaic model

components of membrane free to move, wavy movement, proteins plugged in to make it mosaic

amphipathic

both polar and nonpolar regions

bilayer formation allows for

water on both sides, balance between fluidity and structure

glycolipids

lipids w/ sugar attached instead of phosphate region

glycolipids account for ___% of membrane

5

glycolipids are found on the (inside/outside) of the membrane

outside

glycolipids function

contributes to self recognition

cholesterol accounts for ___% of total membrane lipid

20

cell junctions

held together to create tissues, cells are sugar coated, glycoproteins, acts as glue between cells

gap junctions

connect cells via transport proteins, important for excitable tissue (heart/muscle/nerves, sync electrical activity)

desmosomes

mechanical couplings holding cells together like rivets, wide head on either side

tight junctions

impermeable, no passing through (epithelial cells in intestines, keep digestive enzymes/bacteria out of blood)

3 types of cytosis

phagocytosis, pinocytosis, receptor mediated endocytosis

phagocytosis

engulfing a large particle

pinocytosis

gulping a drop of extracellular fluid

receptor mediated endocytosis

receptors specific for substances bind and the cell ingests

nucleus

site of all hereditary material, encodes for all proteins

organelle

“little organ”, fully enclosed structure inside a cell

mitochondria

produces ATP, inner and outer membrane, many folds (cristae) to increase surface area for ETC

ribosomes

made of protein and RNA, NOT AN ORGANELLE, protein factory, translates mRNA —> proteins, some bound to rough ER others float freely

endomembrane

system of linked organelles that produce/store/export molecules and degrade harmful substances

rough ER

covered in ribosomes and closest to nucleus, produces proteins → packaged into vesicles formed by endocytosis from RER membrane → vesicle empties content into golgi by exocytosis

smooth ER

no ribsosomes, series of tubes filled with enzymes, manufacture lipids/cholesterol/steroid hormones, in intestinal cells absorb/synthesize/transport fats, drug detox, liver cells glycogen → glucose