wk 12

Question 1

location of pro

Answer 1

> 40% sm, >25% organs, >50% cell

Question 2

pro variable in

Answer 2

size, shape, physical properties, physiological properties

Question 3

building block

Answer 3

AA

Question 4

Structure of AA

Answer 4

20 dif, central carbon, carboxyl group, amino group, variable side chain

Question 5

string of AA

Answer 5

polypeptides, connected by peptide bonds, 50+ = pro

Question 6

pro characterized by

Answer 6

number of AA, folding patterns, 1+ polypeptide

Question 7

pro synthesis

Answer 7

central dogma, DNA to mRNA to protein

Question 8

translation

Answer 8

converting mRNA to pro, faciliated by ribosomes

Question 9

selenocysteine

Answer 9

21st AA, derivative of cysteine, sulfur replaced by mineral selenium (macro/micro connection)

Question 10

protein functions

Answer 10

enzymes, hormones, structural, immunoprotein, transport proteins, buffer, fluid balance

Question 11

protein folding

Answer 11

process by which proteins change shape and become progressively more complex, moving from 2 to 3, 3 to 4

Question 12

primary

Answer 12

string of AA connected by peptide bonds, polypeptides

Question 13

secondary

Answer 13

hydrogen bonding within polypeptide of nearby AA, changes shape, alpha helix, beta sheet

Question 14

tertiary

Answer 14

folding together multiple secondary structures, interactions among AA residues or side chains, far away (polarity, side chains, ionic bonds), globular-like structure

Question 15

quaternary

Answer 15

interaction between 2 + tertiary structures, subunits held together by H bonds and electrostatic attractions

Question 16

supramolecular

Answer 16

multiple quaternary structures held together by weak bonds

Question 17

native conformation

Answer 17

protein fully folded and functional

Question 18

chaperones

Answer 18

proteins that aid in protein folding (heat-shock proteins)

Question 19

heat shock proteins

Answer 19

fold proteins right as they come off the ribosome (non-stress), search and rescue misfolded protein during stress or after stressful event (recovery)

Question 20

exercise can do what to heat shock proteins

Answer 20

increase heat shock protein expression

Question 21

protein misfolding

Answer 21

protein sometimes are not folded correctly and chaperones are unable to correct, ideally most will be degraded (not all) Alzheimer’s

Question 22

protein quality control systems

Answer 22

ubiquitin-proteasome system & autophagy

Question 23

ubiquitin-proteasome system

Answer 23

misfolded proteins are tagged with ubiquitin which directs the protein to the proteasome

Question 24

autophagy

Answer 24

degradation pathway for proteins that directs the protein to lysosome

Question 25

AA classifications

Answer 25

essential, nonessential, conditionally essential

Question 26

foods classified as

Answer 26

complete/incomplete proteins, high/low quality proteins

Question 27

essential

Answer 27

can’t be made by body, must be consumed

Question 28

nonessential

Answer 28

body can synthesize

Question 29

conditional essential

Answer 29

becomes essential when the body can’t synthesize enough of non-essential, pregnancy, growth spurts, injury

Question 30

complete

Answer 30

all essential, most animal, soy, quinoa

Question 31

incomplete

Answer 31

not all essential, most plant sources

Question 32

complementary

Answer 32

combining two incomplete pro to obtain all essential

Question 33

research on plant proteins

Answer 33

plants can contain all essential but in too small qualities

Question 34

protein quality

Answer 34

how well protein sources meet nutrition needs, function of essential AA composition, digestibility, and needs of individuals

Question 35

animal products

Answer 35

higher quality, more complete/digestible (90-99%), plant 70-90% due to fiber, soy flour highest protein quality of plant