Test One Review

Front 1

how is positive and negative cooperativity beneficial in nature?

Back 1

pos: makes an on/off switch- response range narrows
neg: change at high ligand doesn't affect function and a protein function can stay constant along a wide range of ligand concentrations

Front 2

transcriptome is altered by:

Back 2

-tissue type
-developmental
-cell cycle
-nutritional status
-drug exposure

Front 3

three methods used to determine 3D structure and their limitations

Back 3

1. X-Ray Crystallography (must form a crystal)
2. NMR (can only use small size)
3. cyto-electron microscope (must use large sized proteins)

Front 4

protomer

Back 4

repeating unit of a protein

Front 5

vesicles in the golgi move from:

Back 5

CIS to TRANS

Front 6

Important features of disulfide bond formation (covalent modification)

Back 6

-oxidation/reduction
-extracellular/RER- stimulates
-cytoplasm/organelles-discourages

Front 7

important features of acetylation

Back 7

usually happens at N-terminus(covers up + charge)

Front 8

important features of glycosylation

Back 8

occurs on side chains with N and O

Front 9

important features of lipoylation

Back 9

occurs as cysteines

Front 10

important features of phosphorylation

Back 10

adds phosphate to OH side chains (ser, tyr, thr)

Front 11

effects of lots of alanines together

Back 11

-small with many allowed regions
-poly-ala = alpha helix

Front 12

effects of lots of prolines together

Back 12

because of the kinks in the background, a random coil might form but usually PPII helix

Front 13

effects of glycines

Back 13

very flexible so it disrupts alpha helices
results in random coils
they are okay if they are scattered

Front 14

______connects beta sheets

Back 14

reverse turns

Front 15

quaternary subunit

Back 15

single polypeptide encoded by one mRNA

Front 16

the effects of motions of proteins

Back 16

could change the function by 1000 fold

Front 17

fibrillar proteins can be made of_____ or ______

Back 17

repeating globular subunits, or long twisted fibers

Front 18

protofilament

Back 18

repeating subunit of fibrillar proteins

Front 19

hydrophobic amino acids

Back 19

alanine, leucine, valine, isoleucine, phenylalanine

Front 20

intrinsically disorded proteins usually function as

Back 20

transcription factors

Front 21

isoforms come from

Back 21

separate ORF or intron/exon splice variants

Front 22

ovumucoid

Back 22

egg white allergen- glycosylation stabilizes fold

Front 23

osmolytes

Back 23

enhance protein folding

Front 24

examples of osmolytes

Back 24

amino acids: pro, ala, taurine
polyols: sorbitol, glycerol
methyamines: TMAO, betaine

Front 25

heat shock proteins

Back 25

found in ER upregulated during stress, fold new proteins and refold misfolded proteins

Front 26

chaperonin

Back 26

found in cytoplasm, large ring of proteins stacked
uses ATP

Front 27

unfoldases

Back 27

target aggregated proteins

Front 28

proteins degrade if--

Back 28

they misfold, chemical damage is present, or for regulation

Front 29

cystic fibrosis

Back 29

protein degrades faster than it can fold

Front 30

native gell separates based on ____ and SDS page separates based on _____,

Back 30

charge, size

Front 31

2D electrophoresis order

Back 31

native
SDS

Front 32

advantages of recombinant protein

Back 32

affects quantity of protein that can be controlled
design amino acid changes

Front 33

disadvantages of recombinant proteins

Back 33

altered folding or post-translational modification
host could also cause contamination

Front 34

characteristics of epithelial tissues

Back 34

cells in close apposition
little/no intercellular substance
lie on basal lamina
form membranes or glands
line all body surfaces, cavities and tubes

Front 35

transitional epithelium is specialized for

Back 35

stretch (urinary system)

Front 36

pseudostratified epithelial found in

Back 36

trachea and epididymis

Front 37

the main function of stratified epithelium

Back 37

mostly protective

Front 38

function of microvilli-
function of cilia-
stereocilia function-

Back 38

absorption(terminal web)
movement(basal body)
absorption

Front 39

basal network

Back 39

network of extracellular matrix proteins that acts as an interface between epithelium and supporting tissue(connective)

Front 40

Pemphigus

Back 40

autoimmune disease-antibodies to desmoglial cells(cadherins)
cells are disrupted and suprabasal blistering as basal cells remain attached to lamina

Front 41

goblet cells/enteroendocrine cells secrete______ from_____

Back 41

goblet: mucins from apical
enteroendocrine: hormones from basal

Front 42

possible qualities of multicellular glands

Back 42

-simple/compound
-tubular/acinar(grapes)
-parenchyma/stroma

Front 43

protein used for when myosin needs to bind actin

Back 43

alpha-actinin

Front 44

muscular dystrophy

Back 44

mutation is dystrophin which is an adapter protein that connects actin to transmembrane proteins of cell membrane

Front 45

mysoin II

Back 45

binds to itself and is used in muscle contraction

Front 46

myosin I

Back 46

used for vesicle transport

Front 47

myosin V

Back 47

used for vesicle transport

Front 48

Griscelli Syndrome

Back 48

mutation that prevents movement of melanosomes

Front 49

movement on MF is (unidirectional/bidirectional).

Back 49

unidirectional--toward the + end

Front 50

MT function as single/or multiple fibers

Back 50

single

Front 51

double MT found in while triple are found in

Back 51

double: cilia
triple: basal bodies and centrioles

Front 52

stathmin

Back 52

sequesters thrombin and when phosphorylated does not do its job

Front 53

MAPs

Back 53

stabilize MTs

Front 54

role of globular proteins in IFs

Back 54

hold together the subunits or influence space between subunits of IF

Front 55

lamins=
vimentin=
desmin=
peripherin=
keratins=
neurofilament=

Back 55

lamins = nuclear lamin
vimentin = mesenchyme
desmin = muscle
keratin = epithelial/skin
peripherin = some neurons
neurofilaments = neurons

Front 56

IFs are localized by_____

Back 56

MTs

Front 57

Epidermolysis bullosa simplex

Back 57

defective keratins(K5/K14) in basal skin layer
severe blistering
mouth/esophageal lining, cornea

Front 58

Charcot-Marie-Tooth

Back 58

abnormal neurofilaments(tangles)
similar to ALS

Front 59

Measures of Health

Back 59

1. Life Expectancy
2. health disparities
3. access to healthcare
4. incidence of diseases
5. quality of life

Front 60

determinants of health

Back 60

individual- biology and behavior
environment-physical and social
policies and interventions
access to quality healthcare

Front 61

what is healthy people 2010

Back 61

nationwide health promotion and diesase prevention agenda

Front 62

affinity

Back 62

how tightly a protein is bound

Front 63

specificity

Back 63

which ligand is bound the tightest

Front 64

Ka units and Kd units

Back 64

Ka = M-1 and Kd = M

Front 65

main goal of allostery

Back 65

regulation! adapt to changing conditions

Front 66

membrane bound proteins show___
fibrillar proteins show____
DNA-binding proteins show___

Back 66

allostery
allostery and cooperativity
cooperativity

Front 67

hill coefficient is related to

Back 67

slope steepness and helps characterize cooperativity

Front 68

___(# of) BPG molecules per tetramer

Back 68

one

Front 69

BPG binds what state of hemoglobin

Back 69

deoxy

Front 70

without BPG, the curve would look like___

Back 70

myoglobin

Front 71

moonlighting rxn of Hb and Mb

Back 71

converts NO to NO3-

Front 72

three types of lipids

Back 72

phospholipids
glycolipids
cholesterol

Front 73

cerebroside

Back 73

single glycolipid

Front 74

ganglioside

Back 74

many glycolipids

Front 75

_________modulates membrane flexibility/fluidity

Back 75

cholesterol

Front 76

type of diffusion allowed

Back 76

lateral

Front 77

what leads to membrane assymetry

Back 77

lateral diffusion
protein islands
cytoskeletal "corrals"
difference in leaflet composition
cholesterol rafts
glycomoietes(exoplasmic)

Front 78

underlying functions of flippase/floppase

Back 78

maintain membrane assymetry

Front 79

_____binds_______which together bind to _______and this _______ smooth muscle cells. This also_____

Back 79

Ca2+ binds calmodulin which together binds non-phosphorylated myosin light chains. This activates smooth muscle cells.

Front 80

2 essential fatty acids in our diet

Back 80

omega 3(lineolenic acid), and omega 6(linoleic acid)

Front 81

enzyme that catalyzes fatty acid to acyl Co-A + AMP

Back 81

acyl-Coa syntehease

Front 82

how is acyl-CoA transported to the matrix for oxidation?

Back 82

carnitine protein carrier

Front 83

the oxidation of unsaturated fatty acid leads to:

Back 83

less FADH2 and less ATP

Front 84

propionyl-CoA is an_____that gets converted to_______

Back 84

odd chain fatty acid- succinyl-CoA using ATP

Front 85

NADPH usually used in_____

Back 85

reduction

Front 86

which kinds of compounds contain the most calories/gram

Back 86

the most reduced

Front 87

how is Acetyl-CoA transported back to the cytosol

Back 87

using pyruvate, oxaloacetate, citrate which is then transported back to the cytosol and releases acetyl-coa

Front 88

ketoacidosis

Back 88

type-1 insulin diabetics
low insulin levels cause fatty acids to be released from the tissue
ketones are synthesized in the liver and used in the brain and other tissues