Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

BMSC 220 > * > Flashcards

* Flashcards

1
Q

amphoteric molecules

A

act as acids or bases depending on environment

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

fat/ triacylglycerol

A
  • glycerol + 3 fatty acid chains (hydrocarbon chain with carboxyl at end)
  • ester linkage (COC)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

fatty acids length

A

14-20 carbons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

saturated (tristearate) / unsaturated (linseed oil)

A
  • Saturated with hydrogens; no C=C double bonds; pack tightly; solid at room temp
  • unsaturated: C=C double bonds; kinks, liquid at room temp (mono and polyunsaturated)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

sickle cell anemia

A

glutamic acid changed to valine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

2 types of secondary structures

A
  • alpha helix
  • beta pleated sheets
  • goal is to maximize hydrogen bonding
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

alzheimers causes

A
  • amyloid plaques (a-peptide aggregates)
  • misfolded Tau proteins (neurofibrillary tangles)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

cell bio approach

A

reductionist (as opposed to functionalist)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

invented the first compound microscope

A

zacharias janssen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

robert hooke

A
  • coined term “cell”
  • used light microscope to look at cork (plant tissue)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

leeuwenhoek

A

first to see living organisms

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

cell theory

A

1) all organisms are composed of one or more cells (schleiden-plants; schwann-animals)
2) all cells arise from pre-existing cells (virchow)
3) the cell is the structural and functional unit of all living things
4) cells contain genetic information (DNA) they pass on to the next cell generation)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

basic propeties of cells

A

1) are alive (cultured cells)
2) highly complex and organized
3) have a genetic program
4) can produce more of themselves
(mitosis + meiosis)
5) acquire and utilize energy
6) carry out chemical reactions
7) engage in mechanical activities
8) respond to stimuli
9) capable of self-regulation (feedback circuits)
10) evolve (LUCA)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

prokaryotes

A
  • unicellular
  • small genome
  • binary fission (asexual, one copy of chromosome)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

flagella

A

both prokar and eukar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

prokaryotic flagellum

A

thin protein filament

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

archaea

A

extremophiles:
- methanogens (convert co2 to methane)
- halophiles
- acidophiles
- thermophiles
- hyperthermophiles

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

mycoplasma

A

only prokaryote without a cell wall

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

protists

A

unicellular

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

differentiation

A

formation of specialized cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

virus

A

intracellular obligate pathogen
- uses host machinery to make proteins
- bacteriophage: virus only infecting bacteria

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

virion

A

more components than virus

  • virus outside of host cell
  • genetic material + capsid (protein coat)
  • +/- envelope (outer lipid membrane)

extracellular virus capable of binding

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

viroid

A
  • RNA
  • smaller than a virus
  • no capsid just the genetic material
  • plants
  • doesnt produce proteins
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

lysogenic viral infections

A

viral DNA inserts into the host cell’s genome (sits there - called a provirus) - can be excised and enter lytic phase when triggered

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

covalent bonds

A

driven by stability - full outermost shell

  • polar (more reactive)
  • nonpolar
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

noncovalent bonds

A
  • ionic bonds
  • hydrogen bonds (hydrogen covalently bound to electroneg atom)
  • hydrophobic interactions
  • van der waals (dipole - holds together neutral molecules)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

bond strength

A

amount of energy required to breaka bond (kJ/mol)

  • covalent stronger in solution than ionic
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

biochemicals

A

compounds produced by living organisms

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

functional groups

A

contain electronegative atoms - make shit polar - makes shit more reactive

  • can be ionized (form charged molecules)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

carbohydrates

A
  • aka glycans
  • function: energy storage, biological construction
  • (CH20)n
  • C-C single bonds backbone
  • water soluble
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

carbs classification

A
  • simple: monosaccharides (glucose, fructose, galactose) + disaccharides (maltose, lactose, sucrose)
  • complex: polysaccharides (starches, fibers, glycogen)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

glycosidic bond

A

covalent bond linking sugars (COC)

  • to each other or lipids in the case of glycolipids
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

disaccharide

A

2 linked sugars

  • oligo (few)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

nutritional + structural polysaccharides

A

Nutritional

  • energy stores
  • glycogen (branched) and starch (branched and unbranched)

Structural

  • cellulose (plant cell wall)
  • chitin (exoskeleton)
  • glycosaminoglycans (GAGs): extracellular space + connective tissue
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

lipids

A

soluble in organic solvent not water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

cholesterol

A

cell memb + precursor of steroid hormones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

proteins

A
  • polypeptide chains
  • amino acids linked via amide/peptide bonds
  • amino acids will have amino + carboxyl group (connected by an alpha carbon)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

cysteine

A
  • thiol group
  • sulfur oxidized –> covalent bond between two cysteine residues (forms disulfide bond which stabilizes proteins)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

primary structure

A

sequence of amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

secondary structure

A

conformation of portions of polypeptide chains - maximizing hydrogen bonding

alpha helix or beta sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

tertiary structure

A

3D conformation of entire polypeptide - eukar proteins will have 2 or more domains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

homologous proteins

A

diff amino acid sequence but still same tertiary structure/ function

  • actin and MreB
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

quaternary

A

multiple polypeptide chains/ subunits

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

molecular chaperones

A

bind to hydrophobic amino acids and help unfolded proteins achieve their 3D conformation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

denaturation of a protein

A

disrupts secondary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

nucleic acids

A

polymers of nucleotides

  • 5 carbon sugar
  • phosphate group
  • nitrogenous base
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

dna vs rna

A
  • OH at carbon 2 in rna
  • rna is single stranded
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

purine

A

adenine + guanine

  • two rings
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

pyrimidines

A

cytosine, uracil, thymine

CUT the PYE

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

thymine has a ____ that uracil does not

A

methyl

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

dna backbone

A

sugar phosphate backbone - forms helix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

ribozymes

A

rna with catalytic activity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

membrane carbohydrates

A
  • glycoproteins: over 90% (glycosylation)
  • glycolipids
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

glycosylation

A

process of attaching sugar to membrane protein

sugar attached to amino acid

  • N-linkage: sugar attached to nitrogen (arginine + asparagine)
  • O-linkage: attached to Oxygen from hydroxyl group (serine + threonine)
54
Q

blood glycolipids

A

glycosidic bond attahching sugar to lipids

  • Blood type A: have enzymes that add N-acetylgalactosamine
  • B: enzymes add galactose
  • AB: both enzymes
  • O: no enzyme
55
Q

factors dicatting proetin movement

A
  • protein size
  • membrane viscosity
  • membrane skeleton
  • neighbouring proteins
  • extracellular interactions
56
Q

RBC membrane skeleton proteins

A
  • spectrin: major component internal membrane skeleton (attached to membrane surface via ankyrin) - linked to other cytoplasmic proetins too
57
Q

western blot

A

chemical SDS denatures proteins and adds a neg charge

  • proteins get separated by size on a gel (polyacrylamide gel electrophoresis - PAGE)
  • primary antibody binds to antigen (protein); secondary antibody with enzyme that produces fluorescence binds to primary antibody - immunostain
58
Q

facilitated diffusion

A

channel
carrier

59
Q

net flux

A

influx - efflux

60
Q

osmosis

A

movement of H2O across a semipermeable membrane from low SOLUTE concentration to HIGH

61
Q

osnolarity

A

[solute] in solution

  • hyperosmotic: more solute, less free water
  • hypoosmotic: less solute, more water
62
Q

turgor press

A

water pressure inside cell - pushes the plasma membrane against the cell wall

63
Q

plasmolysis

A

no water - cell shrinks (hypertonic solution)

64
Q

Aquaporins

A
  • 4 subunits
  • Each subunit has central
    channel (Lined by hydrophobic a.a.)
  • passive facilitated diff
65
Q

channel gating mechanisms

A
  • voltage gated (cell membrane reaching specific amount of voltage triggers opening)
  • stretch-gated (tension gated)
  • phosphorylation gated channel (signal triggers phosphorylation)
  • ligand gated channel (ligand binds to receptor site)
66
Q

channel states

A

open, inactivated, closed

67
Q

bacterial KcsA potassium channel

A

has a selectivity filter (8 C=0 groups and forms a 3.0 A ring in between that only potassium (2.7A) can pass through)

68
Q

carrier proteins

A

principle mode of passive transport for polar organic solutes (glucose, amino acids)

  • rate depends on concentration gradient and number of transporters
69
Q

___________ gradients are generated by active transport

A

electrochemical (gradient stores potential energy)

  • using ATP hydrolysis, light, electron transport, flow of substances going down gradients
70
Q

active trasnport

A
  • primary - use ATP directly (transport protein is both transporter and enzyme since it catalyzes the hydrolysis of ATP; p type pump if it uses atp hydrolysis)
  • secondary - use ATP indirectly
71
Q

electroneutral (active transport) pumps

A

no overall change in cell’s electrical properties

  • parietal cell H+/K+ ATPase: stomach proton pump; acidifies stomach; pumps two protons into stomach in exchange of two K+ in - charge stays same
72
Q

electrogenic (active transport) pumps

A

causes change in electrical properties of cell

  • Sodium potassium pump - 10 membrane spanning helices - conformational changes E1
    &2 change affinity for ions
73
Q

Co-Transport

A

using existing ion gradients for transport

secondary active transport:

  • symporter
  • Antiporter (exchanger)
74
Q

bioelectricity

A

electrical currents and potentials generated by all living cells

75
Q

resting membrane potential

A
  • -70 mV
  • most important ion in RMP: K+
76
Q

depolarization –> action potential

A

+40 mV

77
Q

AP Propagation

A
  • unidirectional + don’t lose strength/intensity
  • speed of neural impulse is greater wth: more axon diameter + myelin
78
Q

nodes of ranvier

A

voltage gated sodium channels - only site where action potentials can be generated - saltatory conduction

79
Q

mitochondria additional roles

A
  • atp production
  • regulation of innate immunity
  • calcium homeostasis
  • apoptosis
  • stem cell regulation
80
Q

high proton concentration in _____ of mitochondria

A

intermembrane space

81
Q

matrix

A
  • krebs cycle enzymes
  • mitochondrial dna (maternally contributed, encodes for 13 proteins)
  • ribosomes
82
Q

ETC and ATP synthase

A

on inner membrane

83
Q

how are the other mitochondrial proteins transported from outside of mitochondria

A

TOM (translocase of outer membrane) and TIM (translocase of inner membrane)

84
Q

glycolysis

A

cytoplasm

  • 2 pyruv, 4 atp, 2 nadh
85
Q

atp structure

A

adenine + ribose + 3 phosphate

86
Q

electron shuttles

A
  • NAD+: nicotinamide adenine dinucleotide - derived from vitamin B
  • FAD+: flavin adenine dinucleotide
87
Q

Pyruvate _____ to Acetyl CoA

A

decarboxylated

88
Q

fermentation

A
  • cytosol
  • forms lactate
  • NAD+ regenerated from glucose
89
Q

main source of energy for cells

A

Krebs cycle (input: oxidized acetyl CoA)

  • Products: 3 NADH (each equals 3 atp), 1 FADH2 (=2atp), 1 GTP (=1atp)
    net gain
  • net gain: 12 ATP
90
Q

pathways that could feed into krebs

A
  • fatty acid cycle: contributes acetyl CoA
  • catabolism of amino acids
91
Q

glycerol phosphate shuttle

A

DHAP (dihydroxyacetone) takes electron from cytosolic NADH and leads to the formation of glycerol-3-phosphate % NAD+ (will takes the electrons across the mitoch)

  • G3PDH (glycerol-3-phosphate dehydrogenase) transfers electron to FAD+
92
Q

cellular respiration

A

glycolysis + krebs + oxidative phosphorylation

93
Q

oxidative phosphorylation

A

2 part process (etc + chemiosmosis)

94
Q

redox potential (oxidation-reduction potential)

A

transfer of electron between a pair causing a charge separation

95
Q

reducing agents ranked according to ______

A

electron transfer potential

96
Q

electron carriers found in different complexes within etc

A
  1. flavoproteins: flavin mononucleotide created by the binding of proteins to FAD (eg. NADH dehydrogenase (complex1)& succinate dehydrogenase (complex2))
  2. cytochromes: heme groups with Fe or Cu metal ions - (3 types: a,b,c)
  3. copper atoms: 3 in a single protein complex (alternate between Cu2+ and Cu3+)
  4. ubiquinone (coenzyme Q): lipid soluble molecule + made of five-carbon isoprenoid units
  5. iron-sulfur proteins: Fe linked to sulfide ions to form iron-sulfide centers (not heme groups)
97
Q

carrier arrangement

A

arranged in order of increasing +ve redox potential

98
Q

proton pump other functions

A
  • takes up adp and p
  • takes up calcium for mitochodnrial fusion
99
Q

tissue types

A
  • nervous
  • connective
  • epthelial
  • muscle
100
Q

basement membrane functions

A
  • structural support
  • tumour invasion
  • cell behaviour
  • angiogenesis (blood vessel development)
101
Q

extracellular matrix proteins

A

more fibrous

102
Q

extracellular matrix molecules

A
  • adhesive proteins (hold cells togther and form organized tissue) - integrins + cadherins + selectins + IgSF
  • structural proteins (tensile and compressive strength) - elastin, keratin, collagen
  • proteoglycans (fibronectin and laminin)
103
Q

collagen

A
  • produced by FIBROBLASTS
  • glycoproteins
  • only in ECM - most abundant protein in body
  • type 1 - most common, bone skin tendon
  • type 2: cartilage
  • type 4: basement membrane (non-helical + terminal globular domains, lattice)
  • 3, triple helix of alpha chains
  • hydroxylation of proline and lysine creates stability - lack causes scurvy
  • staggered alignment
104
Q

tendon collagen

A

parallel, lined up same way

  • cornea ones are arranged perpendicular - prevents refraction + increases tissue transparency
105
Q

proteoglycans

A
  • have amino sugar
  • glycosaminoglycan
  • function: space filler, cushioning, hydration
  • repeating disaccharide structure ABAB
  • acidic + neg charge cuz of amino sugar –> interacts with water and ions - gellike
  • found in basement membranes + cartilage (hydration)
  • eg: fibronectin and lamanin
106
Q

fibronectin

A
  • proteoglycan
  • made of 2 polypeptide chains linked by disulfide bonds
  • many different binding domains - so adds to collagen support framework and attaches cell to ecm
  • role in development of nervous system - informs movement and differentiation of neural crest cells
  • role in formation of salivary gland
107
Q

laminin

A
  • proteoglycan
  • made of 3 polypeptide chains linked by disulfide bonds
  • informs movement and differentiation of neural crest cells
  • Strengthens basement membrane
108
Q

collagen and laminin connected by

A

entactin

109
Q

_____ form the basic insoluble framework of the ECM

A

collagen fibers (laminins form a parallel network)

110
Q

________ degrade ECM components

A

Matrix metalloproteinases (MMP)

111
Q

ECM dynamic properties

A

spatially (ecm fibrils can stretch several times their normal length) and temporally (continual degradation and reconstruction)

112
Q

integrins

A
  • most important cell surface receptor (connects to ecm)
  • glycoproteins
  • alpha and beta chain (heterodimer)
  • 2 confromations (bent is inactivated, upright is activated)
  • talin binds to integrin and anchors cell to ecm and actin cytoskeleton (actin polymerization)
  • functions : adhesion to ecm and other cells + signal transduction inside-out and outside-in (eg. talin and cytoplasmic tyrosine kinases (FAK-src) - phosphorylation)
  • RGD amino acid sequence - binds to cell, blood, ecm, proteoglycans
  • prevent platelet aggregation where not needed
113
Q

Key cellular protein involved in Cell-
ECM adhesion

A

integrin

114
Q

arrangements of integrin

A
  • focal adhesions (macromolecular assemblies forming mechanical links between intracellular actin bundles and the ECM); fxn: ahesion and migration
  • hemidesmosomes: linkage between epithelial cells and basement membrane - keratin and cytoplasmic plaques
115
Q

normal cells

A

integrin-binding

  • malignant are integrin-independent
116
Q

talin

A

anchors cell to ECM and actin cytoskeleton - binds to integrin, causing binding to collagen (ECM) + involved in mobility (actin will pull to whereveer cell is needed to move)

117
Q

mechanotransduction

A

moveement of ecm around cell causes cell to respond too

118
Q

cadherin

A
  • glycoproteins
  • join cells of similar type togetehr
  • calcium dependent
  • loss associated with malignancy
  • give cells tensile strength - prevent from breaking when stretched - hold on to them
  • form: adherens junctions (link cells via actin cytoskeleton; protein plaques connect cadherin to actin) and desmosomes (demoglein and desmocollin bind indirectly to intermediate filaments of the cytoskeleton)
119
Q

adhesion molecules

A
  • integrins
  • cadherins
  • selectins
  • IgSF
120
Q

selectins

A
  • glycoproteins binding specific oligosaccharides (L, E, P selectins)
  • small intracellular and large extracellular portion (membrane-spanning)
  • locations: platelets, leukocytes, endothelial cells
  • functions: cell-cell adhesion + signal transduction
121
Q

immunoglobulin

A
  • have Ig domain
  • cell surface proteins or soluble (antibody)
  • functions: cell recognition, binding, adhesion, neuronal growth and circuitry
122
Q

pemphigus vulgaris

A

antibodies attack desmoglein

123
Q

tight junctions

A

seal extracellular space, seal adjacent plasma membranes

  • major proteins: claudins (adhesion, forms the junction) and occludins (selective permeability)
124
Q

gap junctions

A

intercellular communication

  • connect adjacent cells allowing for rapid communication
  • connexin (has four transmembrane domains) subunits together form connexon (multi-subunit complex)
125
Q

leucocyte recruitment after wound

A
  • selectins
  • integrins
  • IgSF
126
Q

Endomembrane System

A
  • Endoplasmic reticulum (ER)
  • Golgi apparatus
  • Lysosomes
  • Endosomes
  • Vacuoles (plants)

protein synthesis and metabolism

127
Q

constitutive mode of secretion

A

discharged continuously - secretory vesicles

128
Q

SER functions

A
  • Steroid hormone synthesis in endocrine cells
  • Detoxification in liver (Oxygenases, Cytochrome P450 family)
  • Calcium storage and regulated release
129
Q

free reibosomes get proteins to

A

nucleus mitoch peroxisome

130
Q

synthesis of secretory, lysosomal, plant vacuolar proteins

A

amino acid signal sequence (6-15 hydrophobic amino acid residues) in N- terminal portion of polypeptide determines synthesis site

  • nascent polypeptide tells ribosome where to go
  • Signal hypothesis: Proteins have built in “address codes”
  • SRP (using gtp) takes it to ribosome to translocon
131
Q

tail anchored proteins

A

no signal sequence + synthesized in cytoplasm

132
Q

ER associated degradation

A

UGGT checks if protein has folded correctly (conformation sensing enzyme) - tags misfolded protein with glucose, removes mannose - later destroyed by proteasomes

BMSC 220 (1 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions