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46 Cards in this Set

  • Front
  • Back

Nonpolar, non-aromatic

Glycine, alanine, valine, leucine, isoleucine, methionine, proline

Aromatic

Tryptophan, phenylalanine, tyrosine

Polar

Serine, threonine, asparagine, glutamine, cysteine

Negatively charged, acidic

Aspartate, glutamate

Positively charged, basic

Lysine, arginine, histidine

pKa

pH where half of the molecules are deprotonated

Isoelectric point

Average of 2 pKas

Peptide bond formation

Condensation, dehydration

Breaking a peptide bond

Hydrolysis

Apoenzyme

No cofactor

Holoenzyme

Contain a cofactor

Cofactor

Inorganic, metal ion

Coenzyme

Organic, vitamins

Enzyme kinetics, v

vmax[S]/(Km+[S]), kcat[E][S]/(Km+[S])

vmax

[E]kcat

Competitive inhibition

Same y-intercept

Noncompetitive inhibition

Same x-intercept

Uncompetitive inhibition

Parallel lines

Actin

Thin filaments

Negative end

Nucleus

Positive end

Periphery

Myosin

Thick filaments

Kinesins

Bring vesicles to the positive end

Dyneins

Bring vesicles to the negative end

Gs

Stimulate adenylate cyclase, more cAMP

Gq

Activate phospholipase C, more calcium in the cell

Migration velocity

(electric field*net charge)/(frictional coefficient)

Move faster in electrophoresis

Small, highly charged, large electric field

Positively charged protons in isoelectric focusing

Migrate to the cathode

Column chromatography

Nonpolar compounds elute faster

Size-exclusion chromatography

Large compounds elute faster

Bradford protein assay

More protein means more blue dye

Epimer

Different at one chiral center

Alpha anomer

Axial, down

Beta anomer

Equatorial, up

Sucrose

Glucose, fructose

Lactose

Galactose, glucose

Maltose

Glucose, glucose

Saturated fatty acid

Solid

Unsaturated fatty acid

Liquid

Sphingomyelin

Phosphodiester bond

Glycosphingolipid

Glycosidic linkage

Monoterpene

Two isoprenes

Sesquiterpene

Three isoprenes

Purine

Two rings, adenine, guanine

Pyrimidine

One ring, cytosine, thymine, uracil