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CHEMISTRY NOTES > lipids > Flashcards

lipids Flashcards

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1
Q

simple lips and complex lipids

A

waxes fat oil - S
PHOSPHILIPIDS GYLCOLIPIDS STEROID-complex

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2
Q

saponifiafiable of lipid examples

A

waxes triacyglycerole triglycerides

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3
Q

nonsaponifiable lipid

A

no OH BOND NO ESTER

STEROID
TERENE

no fatty acid

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4
Q

lipids function

A

structural components cell membranes
chemical messagerrs
insulation
protective coating
shock absorbers
storage and transport fuel

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5
Q

saturated fatty acids

A

PSS
PAMISTIC STEARIC SATURATED

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6
Q

unsaturated fatty acid

A

oleic acid
Linoleic acid

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7
Q

fatty acid are

A

long branch hydrocarbons with carboxl group

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8
Q

lipid functional group

A

ester

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9
Q

triacygylcerol make up most lipid in our food

A

true

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10
Q

tryacylglycerol

A

3OH +Gylcerol +3fatty acid
3 esters

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11
Q

hydrogenation

A

alkene +H2 >Alkane break double bond , you add H’s

can also form alcohol

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12
Q

fluid mosaic model describes the plasma membrane of all cells

with cis double bond carbohydrates cholesterol selective permeability

A

true

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13
Q

protein are held by

A

amide bond

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14
Q

function of protein (build stuff in body

A

stuctural collagen keratin ( hair skin )

enzyme catalysts

hormones regulate metabolism and nervous system

protection - immunoglobulin (antibodies
transport hemoglobin

storage - myoglobin

regulation - gene expression

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15
Q

type of proteins

A

fibrous insoluble in water provide structure of cell

globular compact- spherical shape -soluble transport protein

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16
Q

amino acid are neurotransmitters?

A

yes

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17
Q

glycine

A

G
NONPOLAR
Has H (side)

achiral

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18
Q

alanine

A

nonpolar
CH3 ( G side)

A

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19
Q

cysteine

A

polar - neutral
HS - CH2
C

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20
Q

glutamic acid

A

acidic - Polar

E

O—C=O-ch2ch2

(ch2)COOH

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21
Q

lysine

A

lys
K

Basic polar
(Ch2)4NH2

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22
Q

what is a zwitteriom

A

A molecule that has both positive and a negative charge, but we remain electrically neutral overall
act as buffer

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23
Q

only L AMINO ACID OCCUR IN PROTEIN

A

true

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24
Q

which amino acid has chiral except one

A

all amino acid have chiral except glycine who only H

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25
peptide bond
are amides formed by joining the amino group ( A with carboxyl group a dehydration process +H20
26
peptide hydrolysis
dipeptide hydrolysis > amino acid (break down of it
27
alanine +gylcoine name them
dipeptide
28
primary structure amino acid
about the number & sequence of it join by the peptide bond straight line
29
secondary structure
held by hydrogen bond alpha helix beta pleated sheet snake shape
30
palmitic stearic acid contain how many carbon
p 16 s18
31
the fold and bend
tertiary structure with disulfide hydrophobic salt bridges
32
quaternary
partial relationship between two or more polypeptide chains ; come together as an intact protein
33
salt bridges
attraction has both full positive and full negative charge occur on side chain Glutamic acid and lysine
34
how much disulfide bond insulin do human have
3
35
hydrogen bond form between
N-H and c=O
36
desaturating agents
heat microwave ultraviolet light acid base heavy metal organic solvent - hydrophobic interaction detergents
37
protein contain elements like
CHON S
38
denaturation
the disorganized of protein which results in the loss of the protein characteristics doesn’t effect primary structure therefore not hydrolysis but effect 2-3-4
39
0.8 gram of protein per kg so if a person weight 55kg u gon 55*0.8
true
40
ninhydrin
reagents turn blue in presence of free amino acid
41
the treatment of protein with NAOH AND CUSO4 make purple
biuret
42
what is enzymes
enzymes are protein that catalyzed biological reaction
43
Conjugate + cofactor =
Haloenzyme formed
44
A conjugate protein composed of
protein& non protein parts
45
Haloenzyme
whole enzyme complete enzyme
46
conjugated enzymes ex:
apoenzyme - protein portion cofactor nonprotein part
47
type of cofactors
metal ions inorganic cu2 Fe2 K+ zn + man coenzyme- organic molecules B VITAMINS
48
molecules of a substrate combined with its enzyme
enzyme substrate complex
49
enzyme PH BODY TEMP!
5-7 ph 37C
50
competitive inhibition
An inhibitor binds to active site deactivating the enzyme compete w substrate ( reactant) for active sites
51
non-competitive inhibition
an inhibitor bind to a non-active site on the enzyme, changing its shape, deactivating the enzyme
52
Cofactor remove frm enzyme make it
Apoenzyme (protein part)
53
substrate are
The reacting that will undergo chemical change and the enzyme shape
54
Active site is
part of the enzyme where reaction. Take place in the subtract fits.
55
describe lock key and induce fit model
lock and key exact fit no change induce fit is changes shape so enzyme could fit on it
56
cyanide ion
form complex Cooper ion effect, cellular respiration
57
Heavy metals
react with SH group, causing protein dinner denaturation
58
arsenic
mimics phosphorus react with SH bond
59
Nerve poison
inhibit neurontransmitters ex : PO4^-3
60
Toxins
botulinus bacillus paralysis
61
if the temperature greater than 40c what happens to protein
denature protein and deactivate enzyme
62
hormones definition
Are produced by the endocrine gland den transported through the bloodstream respond to stimulus they act as control agent regulate growth and sexual function
63
polypeptide
insulin which produce a signal that allows glucose to be transported into the cell circulated in the bloodstream that binds w receptor insulin that send signal let glucose transport in the bloodstream to bind w receptor
64
Steroids
from cholesterol cause itching and redness in addition to suppression of the immune system
65
neuron transmitters
are chemical made in neuron which carry signal to the next nerve cell.
66
acetylcholine
is the neuron transmitter of the automatic system
67
all amino acid are L amino acid except
glycine
68
crystalline
their amino acid have high melting point more soluble in water exist as a zwitterion 262c
69
hydrophobic interactions
fold to avoid water which affect the shape of the protein
70
electrophoresis
A method of separating an analyzing protein, different ion migrate, a different speed through an electric field ( makin them move through electric field )
71
regulatory genes
regulate the production of the Appoenzyme stop the transcribing & make protein unable to make
72
Regulatory enzymes
product of the reaction that act as an inhibitor make it negative feedback
73
oilec and linoleic are what type of saturated
monounsaturated-O Polyunsaturated-L
74
Only L amino acid occur in protein & Glycine occur to but not L amino acid
true
75
aldehyde goes under oxidation form
carboxylic acid
76
aldehyde or ketone +. 2 mold of Alcohol =acetal
77
functional group of hemiacetal acetal
oH Or Hemi. R1R2c(OH) R2C(OR')2 Acetal

CHEMISTRY NOTES (11 decks)

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