Biochem Final

Front 1

Pneumonic for glycolysis

Back 1

Good gracious father franklin did good by preparing pickled penguin pies

Front 2

Products of glycolysis in order

Back 2

Glucose, Glucose 6 phosphate, fructose 6 phosphate, fructose 1,6 bi phosphate, dehydroxy acetone phosphate, glyceraldehyde 3 phosphate, 1,3 bi phosphoglycerate, 3 phosphoglycerate, 2 phosphoglycerate, phosphoenolpyruvate, pyruvate

Front 3

What steps have ATP consumed

Back 3

Glucose -> glucose 6 phosphate

Fructose 6 phosphate -> fructose 1,6 biphosphate

Front 4

What steps in glycolysis is energy produced

Back 4

glyceraldehyde 3 phosphate -> NADH

1,3 biphospho glycerate -> 3 phosphoglycerate produces an ATP for each molecule (2ATP)

phosphoenolpyruvate -> pyruvate - 1 ATP per molecule - 2 ATP total

Front 5

How many net ATP are produced for each molecule of glucose

Back 5

2 go in, 4 come out - 2 net ATP plus 2 NADH

Front 6

salting out

Back 6

using ammonium sulfate or polyethylene glycol which compete for water with the organelle of interest - part of interest is salted out

Front 7

Molecular sieves

Back 7

contain pores of different sizes - molecules too larger pass through unimpeded - smaller linger for a while and are passed later

Front 8

Ion exchange chromatography

Back 8

depends on net charge - negative impede positive charges and the reverse

Front 9

affinity chromatography

Back 9

depends on specific interactions b/w molecule and compound it reacts with. ex - enzyme binding w/ substrate or bonded w/ antibody - usually applied later

Front 10

Discontinuous electrophoresis

Back 10

using a gel slab to separate based on size and charge

Front 11

specific activity

Back 11

ratio of biological activity to the mg of total protein - increase as purification progresses

Front 12

assay

Back 12

process of determining specific activity

Front 13

stereospecific

Back 13

a stereospecific reaction can proceed through only 1 stereoisomer (differs in 3D structure)

Front 14

denaturation

Back 14

reversible or irreversible loss of higher macromolecular structures by chemical or physical means, leaving the primary structure intact

Front 15

glycoprotein

Back 15

proteins with one or more carbohydrate moieties covalently attached to the polypeptide chain;

Front 16

endergonic

Back 16

not spontaneous - energy put into the system

Front 17

active site

Back 17

place where the substrate must bind in order to activate the enzyme

Front 18

cytochrome

Back 18

are heme iron-containing electron transport proteins

Front 19

phosphofructokinase

Back 19

main regulatory enzyme in glycolysis

Front 20

quaternary structure

Back 20

several different polypeptide chains interacting w/ eachother

Front 21

structure of amino acid

Back 21

NH3+-CH-COO-, with an R group also attached to the middle carbon

Front 22

peptide bond

Back 22

bond b/w two amino acids

Front 23

distinguish b/w L and D amino acids

Back 23

the optical activity of the isomer of glyceraldehyde from which that amino acid can theoretically be synthesized

Front 24

proteins

Back 24

responsible for shape, structure and chemical activities occuring inside cell

Front 25

amphoteric

Back 25

possessing both acidic and basic group

Front 26

primary structure

Back 26

order of amino acids in the polypeptide chain

Front 27

secondary structure

Back 27

spatial relationship of the main chain - may assume a helical or sheet structure. Hydrogen bonding b/w residues of the chain stabalize

Front 28

tertiary structure

Back 28

chemical reactions b/w the side groups- superfolding

Front 29

quarternary structure

Back 29

interactions b/w several polypeptide chains each with their own 1, 2, 3 structure.

Front 30

urea

Back 30

helps in denaturing of the proteins

Front 31

zwitterions

Back 31

compounds that have a positive charge on one atom and a negative charge on another - amino acids

Front 32

types of interactions in the tertiary structure

Back 32

covalent bonds, hydrogen bonding, salt bridges, hydrophobic interactions, metal ion coordination

Front 33

Ways to denature

Back 33

heat, urea, detergents, acids/bases, salts, heavy metals, alcohol

Front 34

enzymes

Back 34

most of the time are proteins - catalysts - only affect the RATE of reaction - does not influence final equilibrium - affects forward and reverse equally

Front 35

ways to affect enzymes

Back 35

pH - may interfere w/ degree of ionization of amino acid side change - change the interactions b/w side chains and folding pattern

mutations - incorrect amino acid placement

urea, heat, concentration, competitive/noncompetitive inhibitors

Front 36

competitive inhibitors

Back 36

compete with substrate for attachement to binding site

Front 37

non competitive inhibitors

Back 37

prevent binding by interacting with teh enzyme molecule at a site other than the binding site

Front 38

catalysts

Back 38

speed up a reaction

Front 39

energy barrier

Back 39

enzymes act by lowering energy barrier and allowing the reaction to proceed

Front 40

low specificity

Back 40

only with teh type of linkage b/w A and B - esterase may only hydrolyze many esters irrescpective of the alcohol and acid moeties

Front 41

group specific

Back 41

not concerned w/ linkage but will work on specific groups related to B in the A-B linkage

Front 42

absoulte specificity

Back 42

each substrate defined absolutely - no variation

Front 43

enzyme regulation

Back 43

feedback control - formation of product inhibits