TEST 2 Flashcards
(125 cards)
1
Q
carb functions
A
energy source
structure
cell-cell recognition
2
Q
monosaccharides
A
-must be aldehyde or ketone
-must be polyhydroxy (2 or more OH groups)
-ends in ose
-has 3 or more carbons
-D chirality
3
Q
D chirality
A
-based on chiral carbon furthest from aldehyde or ketone group
-OH on the right
4
Q
L chirality
A
-based on chiral carbon furthest from aldehyde or ketone group
-OH on the left
5
Q
aldehyde carbohydrates
A
aldose
6
Q
ketone carbonhydrates
A
ketose
7
Q
constitutional isomers
A
-chemicals with the same number of each atom
-different structures
8
Q
A
L pentose aldose
9
Q
enantiomers
A
mirror images
10
Q
diasteriosmers
A
isomers that arent mirror images
-anomers
-epimers
11
Q
epimers
A
differ at only one chiral carbon
12
Q
anomers
A
isomers that differ at a new asymmetric carbon formed on a ring closure
13
Q
what is the relation between 2 chemicals that differ between 2 or more chiral carbons?
A
no relation
different chemicals
14
Q
A
furan
15
Q
A
pyran
16
Q
alpha anomer
A
the OH group is attached below the final group furthest from the inital ketone/aldehyde group
17
Q
beta anomer
A
the OH group is attached to the same plane in the ring as the final group in the pre ring form
The oh group is created through the destruction of the ketone/aldehyde group into an oh group
18
Q
anomeric carbon?
A
A, anomeric carbons must be bound to the oxygen and have a hydroxyl group
18
Q
ether bonds are made from what
A
2 OH groups done through condensation reactions
18
Q
how to tell if a ring is an aldose or a ketose
A
-if the anomeric carbon is bonded to a carbon chain outside of the ring its a ketose
-if the anomeric carbon is bonded to only a hydrogen and a hydroxyl group its an aldose
19
Q
what type of sugars where sugar 1 and sugar 2
A
sugar 1 beta
sugar 2 alpha
20
Q
how to identify what type of bond 2 sugars have?
A
-if both carbons are anomeric idenitfy the configuration for both and state that in answer
-find the number of carbon that the carbon in the bond is
-put it in the following format
-A1-B4
-A1-4
-B1-5
21
Q
Cellulose
A
most abundant organic compound
Beta 1-4 linkages
unbranched
cant be digested
22
Q
starch (Amylopectin)
A
glucose monomer
alpha 1-4 linkages
alpha 1-6 linkages for branches
(1 branch every about 30 residues)
can be digested
23
starch (amylose)
glucose monomer
alpha 1,4 linkages
unbranched
can be hundreds of monomers long
can be digested
24
Glycogen
glucose monomer
alpha 1-4 linkages
alpha 1-6 linkages for branches
(1 branch for about every 10 residues)
25
Homo polymers
same monomers repeating over and over
26
carb cell cell recognition example
Blood type (ABO)
27
lipid functions
energy fuel and storage
membrane components
hormones
28
fatty acids
long chain hydrocarbons
terminates w carboxylic acids
(usually ends w even # of C's and may have double bonds)
ends in oate or itic acid
29
fatty acid functions
-fuel
-building blocks for membranes
-carbons in fatty acids are reduced than carbohydrates
this helps fats yield more energy than carbs
30
fatty acid numbers system
can be designated by number of carbons and double bonds in the following fashion
18C 2 double bonds = (18:2)
14C 0 double bonds = (14:0)
31
⍵ carbon
always last carbon on the fatty acid chain
32
⍺ carbon
carbon in second position from carboxylic acid starting the fatty acid chain
33
Δ in fatty acids
Δ then a number inticates at which locations on a fatty acid chain double bonds are located
so Δ6 is a double bond at the sixth carbon
34
how to count chain
count double bonds on a fatty acid chain from the inital carbon on the chain which is usually the carboxylic acid's carbon
35
how to count chain from ⍵
count double bonds on a fatty acid chain from the last carbon on the chain (NOT THE CARBOXYLIC ACID END)
only refer to the position of the closest double bond
if the fatty acid has more than 1 disregard the others
36
saturated fatty acid characteristics
higher melting points
37
unsaturated fatty acid characteristics
lower melting points
double bonds
cis configuration not trans
38
mammals cant produce double bonds beyond what carbon chain length
carbon 9
39
what is a triglyceride
3 ester linkages to tri carbon chain
40
Sphingolipids
carbon chained linked to an amide then to glycerol
only 1 hydrocarbon chain
41
isoprenoids
vitamins KADE
chlorophyll
terpenes
heme
42
cholesterol
-precursor to biologically active steroids
-helps in cell signaling and lipid rafts
43
phospholipid behavior
immediately aggregate to form lipid bilayer
44
phospholipids
amphipathic molecule
nonpolar tail
polar head
45
sphingolipid
46
integral membrane proteins
bound into the tail/hydrocarbon chain
span most of bilayer
only released when bilayer is disrupted
47
peripheral membrane protein
bound into the head of the phospholipi
48
lipid component of cell membrane
50-75%
49
protein component of cell membrane
25-50%
50
fluid mosaic model
2D representation of the cell membrane
phospholipids and all proteins included
51
movement of proteins and phospholipids in bilayer
can diffuse laterally but can not flip to other side of membrane
52
uniport
Movement of one substance across membrane
53
Symport
Uses downhill flow of one species to drive the uphill flow of a
different species in the same direction across a membrane
cotransport
active transport
54
antiport
Couples uphill flow of one species to downhill flow of another
species in opposite directions across a membrane
cotransport
active transport
55
Passive Transport
usually lipophilic
simple diffusion
high to low concentration across a plasma membrane
56
Facilitated diffusion
moving substances against concentration gradient
57
Primary Active Transport
-Transport AGAINST a concentration gradient- requires the input of energy
(generally from ATP)
58
Secondary Active Transport
-Movement of one substance against its concentration gradient, while moving something else toward its concentration gradient
59
Na+/K+ sodium ion pump
-3Na+ out
-2K+ in
-both against concentration gradient
-creates electrochemical gradient
-1/3 of an animals resting energy is utilized doing this single process
-antiport
60
downhill flow
high to low
61
uphill flow
low to high
62
membrane protein functions
cell boundaries
transport
catalysis
receptor
63
signal transduction pathway by receptor/catalysis proteins
1) release of primary messenger
2) reception of primary messenger- usually outside of cell
3) relay of info by second messenger- signal amplified in cell
4) activation of effectors that alter physiological responce
5) termination of signal
64
needed omega fatty acids
omega 3 and omega 6
65
beta carotine is converted to what
vitamin A
66
triglycerides are linked by what
ester linkages
67
active vs facilitated transport
active-requires energy, across electrochemical gradient
facilitated- passive movement with electrochemical gradient
68
minimum number of carbons needed for monosaccaride
3
69
what lipid stores energy
triglycerides
70
monosaccarides are linked by what
ether linkages
71
if this monosaccaride were to turn into a ring what carbons would be involved? How?
Carbon 5 attacks carbon 1
72
G-protein coupled receptors
-alpha beta and gamma
-unactivated state- GDP bound (OFF)
-conformational changes in cytoplasmic domain cause release of GDP and bindiing of GTP (ON)
-adenylyl cyclase converts ATP to cAMP (second messengers)
-cAMP regulates activities of protein kinase A
-kinases- enzymes that phosphorylate a substrate using ATP
73
epinephrin cell pathway
1) epinephrin binds to cell receptor
2) receptor causes replacement of GDP with GTP by activated alpha subunit of g protein
3) alpha subunit activates adenylyl cyclase
4) adenylyl cyclase creates cAMP
5)PKA is activated by cAMP
6)phosphorylation of proteins by pka causes cell response to epinephrin
7)cAMP is degraded and terminates responce
74
side effects of increased cAMP and kinase activity
degradation of glycogen/cellulose
stop synthesis of glycogen
75
gtpase activity
GTP hydrolyzes to GDP
degredates GTP to terminate signal
76
insulin signal transduction pathway
1) insulin binds to receptor
2) tyrosine kinase activity, it cross phosphorylates itself
3) phosphoylated tyrosine kinase domains attracted other substrates and phosphorylates them
4)phosphoylated IRS proteins regulate other proteins, stimulates glycogen synthesis
5) terminates signal through phosphatases that removes phosphates on the proteins
77
cholera
prevents G protein from GTPase activity
signal will always be on
78
pertussis
stops G protein GDP to GTP exchange
cant turn on pathway
79
catabolic pathways
reactions that convert energy from
fuels to a useful form
break down
80
anabolic pathways
reactions that require inputs of energy
build up
81
3 fundamental needs for energy
performance of mechanical work
active transport of ions and molecules
synthesis of biomolecules and macromolecules
82
ΔE = q + w
q = heat
w = work
83
spontaneous reactions
-∆G
exergonic
84
non-spontaneous reactions
+∆G
endergonic
85
∆G provides no info abt what
the rate of the reaction
86
∆G
energy change associated as a reaction goes from initial equailibrium to final equilibrium
87
more negative ∆G
larger value of Keq
88
more positive ∆G
smaller value of Keq
89
sphingolipid functions
play a role in cell to cell signaling
90
how is an insulin signal propagated through the cell
through phosphorylation of insulin receptor substrates
91
in the epinephirin pathway what does adenylyl cyclase do to amplify the signal
it creates cAMP
92
adenylyl cyclase
converts ATP to cAMP (second messengers)
-cAMP regulates activities of protein kinase A
93
keq < 1
reactants favored at equilibrium
94
keq > 1
products favored at equilibrium
95
there must be an intermediate in common in order for what
coupiing of reactions
96
Strategies for capturing and transfering energy
phosphoryl group transfer
activated carriers of electrons
activated carries of two carbon units
97
phosphoryl group transfer
-method of capturing and transfering energy
-high phosphoryl transfer potential compounds generated from metabolism of fuel molecules used to power synthesis of ATP
-ATP donates phosphoryl group to facilitate the metabolism of other molecules
98
what dont lipids do
catalyst
99
what molecule is a two carbon carrier?
coenzyme A
100
ATP
very stable
high activation energy
very favorable to lose 3rd phosphate group -30J
101
activated carriers of electrons
method of capturing and transfering energy
oxidation and reduction reactions
reduced form NADH NADPH FADH2
oxidized form NAD NADP+ FADH+
102
oxidation reduction actions
half reactions that occur together
103
oxidation
loss of electrons
104
reduction
gain of electrons
105
Cu 2+ oxidation state
+2 oxidation state
106
CO2 is what
fully oxidized
107
CH4 is what
fully reduced
108
how to find oxidation state
H are +1 in oxidation state
O are -2 in oxidation state
109
methane oxidation state
-4
4+ hydrogens means the carbon must be negatively charge 4
110
methanol oxidation state
-2
4+ hydrogen charge + -2 oxygen charge = 2+ overall charge bound to carbon therefore carbon must have a -2 oxidation state
111
formaldehyde oxidation state
0
2+ hydrogen charge + -2 oxygen charge = 0 overall charge bound to carbon therefore 0 overall oxidation state
112
formic acid oxidation state
+2
2+ hydrogen charge + -4 oxygen charge = -2 overall charge bound to carbon therefore +2 overall oxidation state
113
carbon dioxide
+4
-4 oxygen charge = -4 overall charge bound to carbon therefore +4 overall oxidation state
114
two electron carriers
NAD+/NADH
NADP+/NADPH - often used as electron donor in biosynthesis
115
NAD oxidized reduction states
NAD+/NADH
116
NADP oxidized reduction states
NADP+/NADPH
117
FAD oxidized reduction states
FAD/FADH2
118
single electron carrier
FAD/FADH2 can still be a two electron carrier
119
activated carriers of two carbon units
method of energy transfer and capture
uses Acyl CoA/acetyl CoA
120
NADH and NADPH precursors
vitamin B3/ nicotinate
121
FADH2 precursor
Riboflavin/vitamin B2
122
CoA precursor
Pantothenate/vitamin B5
123
