lipids Flashcards
simple lips and complex lipids
waxes fat oil - S
PHOSPHILIPIDS GYLCOLIPIDS STEROID-complex
saponifiafiable of lipid examples
waxes triacyglycerole triglycerides
nonsaponifiable lipid
no OH BOND NO ESTER
STEROID
TERENE
no fatty acid
lipids function
structural components cell membranes
chemical messagerrs
insulation
protective coating
shock absorbers
storage and transport fuel
saturated fatty acids
PSS
PAMISTIC STEARIC SATURATED
unsaturated fatty acid
oleic acid
Linoleic acid
fatty acid are
long branch hydrocarbons with carboxl group
lipid functional group
ester
triacygylcerol make up most lipid in our food
true
tryacylglycerol
3OH +Gylcerol +3fatty acid
3 esters
hydrogenation
alkene +H2 >Alkane break double bond , you add H’s
can also form alcohol
fluid mosaic model describes the plasma membrane of all cells
with cis double bond carbohydrates cholesterol selective permeability
true
protein are held by
amide bond
function of protein (build stuff in body
stuctural collagen keratin ( hair skin )
enzyme catalysts
hormones regulate metabolism and nervous system
protection - immunoglobulin (antibodies
transport hemoglobin
storage - myoglobin
regulation - gene expression
type of proteins
fibrous insoluble in water provide structure of cell
globular compact- spherical shape -soluble transport protein
amino acid are neurotransmitters?
yes
glycine
G
NONPOLAR
Has H (side)
achiral
alanine
nonpolar
CH3 ( G side)
A
cysteine
polar - neutral
HS - CH2
C
glutamic acid
acidic - Polar
E
O—C=O-ch2ch2
(ch2)COOH
lysine
lys
K
Basic polar
(Ch2)4NH2
what is a zwitteriom
A molecule that has both positive and a negative charge, but we remain electrically neutral overall
act as buffer
only L AMINO ACID OCCUR IN PROTEIN
true
which amino acid has chiral except one
all amino acid have chiral except glycine who only H
peptide bond
are amides formed by joining the amino group ( A with carboxyl group
a dehydration process +H20
peptide hydrolysis
dipeptide hydrolysis > amino acid (break down of it
alanine +gylcoine name them
dipeptide
primary structure amino acid
about the number & sequence of it join by the peptide bond
straight line
secondary structure
held by hydrogen bond
alpha helix
beta pleated sheet
snake shape
palmitic
stearic acid contain how many carbon
p 16
s18
the fold and bend
tertiary structure
with disulfide
hydrophobic
salt bridges
quaternary
partial relationship between two or more polypeptide chains ; come together as an intact protein
salt bridges
attraction has both full positive and full negative charge occur on side chain
Glutamic acid and lysine
how much disulfide bond insulin do human have
3
hydrogen bond form between
N-H and c=O
desaturating agents
heat
microwave
ultraviolet light
acid base
heavy metal
organic solvent - hydrophobic interaction
detergents
protein contain elements like
CHON S
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
0.8 gram of protein per kg
so if a person weight 55kg u gon
55*0.8
true
ninhydrin
reagents turn blue in presence of free amino acid
the treatment of protein with NAOH AND CUSO4 make purple
biuret
what is enzymes
enzymes are protein that catalyzed biological reaction
Conjugate + cofactor =
Haloenzyme formed
A conjugate protein composed of
protein& non protein parts
Haloenzyme
whole enzyme
complete enzyme
conjugated enzymes ex:
apoenzyme - protein portion
cofactor nonprotein part
type of cofactors
metal ions inorganic
cu2 Fe2 K+ zn + man
coenzyme- organic molecules B VITAMINS
molecules of a substrate combined with its enzyme
enzyme substrate complex
enzyme PH BODY TEMP!
5-7 ph
37C
competitive inhibition
An inhibitor binds to active site deactivating the enzyme
compete w substrate ( reactant) for active sites
non-competitive inhibition
an inhibitor bind to a non-active site on the enzyme, changing its shape, deactivating the enzyme
Cofactor remove frm enzyme make it
Apoenzyme (protein part)
substrate are
The reacting that will undergo chemical change and the enzyme shape
Active site is
part of the enzyme where reaction. Take place in the subtract fits.
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
cyanide ion
form complex Cooper ion effect, cellular respiration
Heavy metals
react with SH group, causing protein dinner denaturation
arsenic
mimics phosphorus react with SH bond
Nerve poison
inhibit neurontransmitters
ex :
PO4^-3
Toxins
botulinus bacillus
paralysis
if the temperature greater than 40c what happens to protein
denature protein and deactivate enzyme
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
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
Steroids
from cholesterol cause itching and redness in addition to suppression of the immune system
neuron transmitters
are chemical made in neuron which carry signal to the next nerve cell.
acetylcholine
is the neuron transmitter of the automatic system
all amino acid are L amino acid except
glycine
crystalline
their amino acid have high melting point
more soluble in water
exist as a zwitterion
262c
hydrophobic interactions
fold to avoid water which affect the shape of the protein
electrophoresis
A method of separating an analyzing protein, different ion migrate, a different speed through an electric field ( makin them move through electric field )
regulatory genes
regulate the production of the Appoenzyme
stop the transcribing & make protein unable to make
Regulatory enzymes
product of the reaction that act as an inhibitor make it negative feedback
oilec and linoleic are what type of saturated
monounsaturated-O
Polyunsaturated-L
Only L amino acid occur in protein & Glycine occur to but not L amino acid
true
aldehyde goes under oxidation form
carboxylic acid
aldehyde or ketone +. 2 mold of Alcohol =acetal
functional group of hemiacetal acetal
oH Or Hemi. R1R2c(OH)
R2C(OR’)2 Acetal
