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how is subcellular things studied today
autoradiography,microscopy and centrifugation
compound light microscope
1.diaphragm—controls the amount of light entering
2.course or fine adjustment knob—-controls the focus
phase contrast microscope
tradeoff os seeing living organism but almsot no contrast or focus at specific organs
most visually focused microsocope
electron microscope—but leads to death of an organism inorder to examine them
uses heavy metals like OsO4
light and electron microscope difference
ranges in nanometers(wavelength of lights) and picketers(beam of electrons)
electron microscope’s biggest achievement
differentiate between outer and inner mitochondrial membranes
autoradigraphy
use of x rays and radio frequency rays
based on how biochemical reactions occur with the different component of the body and when put in dark shows areas where a reaction occurs to create a better x ray image
centrifugation
works on density and shape difference and how greater force shows greater effect on the greater density and thus pulling it down more
more dense-ribosomes and
less dense —mitochondria and lysosomes
prokarya
contains a bacterial genome insde a nucleoid region but also had small pieces of DNA called plasmid
plasmids are beneficial because
helps differentiate a bacterial strain that is suspectible to an antibiotic and one that is resistance to it
plasmids can reproduce and carry multiple plasmids to next generation for carrying on the antibiotic resistance
spherical and rod shaped bacterias are
staphylococcus aureus and escherichia coli
we always look for features found specifically in
a specific bacteria in that drug to kill it like arithromycin for ear infection kills a specific bacterial ribosome smaller than the eukarya ribosome
largest to smallest proteins making up the cytoskeleton
Microtiubules >intermediate > actin
phospholipid bilayer has
protein and lipid rafts
hydrophobic tail but a hydrophilic head
major component of hydrophobic tail
cholesterol—helps maintian the membrane fludiity and stiffness and produces steroid hormones in animals
more non polar means
more easier to transverse in the hydrophobic nature of the core
two imp. proteins
transport
CAMs(cell adhesion Molecules)—helps with cell development and differentiation
nucleus is
helps direct protein synthesis and carries genetic blueprint during cell replication
nucleolus helps with
sysnthesis of rRNA
ribosomes gives out the products to
endoplasmic reticulum
rough and smooth endoplasmic reitculum
production and sorting of protein products while smooth helps with detoxification of drugs or synthesis of lipid
golgi helpsw ith
repackaging material recieved from the smooth ER and further direct them to cell surface
where they travel by secratory vesicles (process of exocytosis)
vesicles are helping with
wrapping and sending out materials (trasport ) and store things that are processed,secreted or digested
lysosomes help with
recycling material ,it kind of acts as a garbage dump so sequester the hydrolytic enzymes(Endosomes) to not damage the cell—kind of digests them and also can cause autolysis (cell death)
mitochondria
-outer -contains material for respiration
-inner -contains material for ETC (enzymes and molecules)
cristae function ?
increases surface area for all the enzymes to sit in
which organelle is passed only from mother
MITOCHONDRIA
apoptosis linked with mitochondria how?
certains enzymes might be releases int eh etc (which are not supposed to) during apoptosis
Mitochondria are
semiautonomous
chloroplasts
have their own dna and may ahve evovled by symbiosis (like mitochondria)
peroxisomes and glycoxisomes
present in animal and helps catalyze the detoxification in liver and converting food to fuel
glycoxisomes are in plants and they also help break down food to usable forms
cell wall type in plants and fungi
cellulose and chitin
centrioles
present only in animals and help in spindle formation
also responsible for the highway system like microtubules
cytoskeleton contains:
intermediate,microtubules and microfilamnets
microfilament
made of actin ,is solid and forms smallest road during muscle contraction
in muscle onctraction—-actin meets myosin
helps with movement of materials
microtubules
forms the largest roads ,are hollow and made of tubulin
helps with seperation of chromosome in division
cilia and flagella movement to trap foreign particles
intermediates help with
maintaining overall integrity of cytoskeleton and made of fibres
osmosis
movement of water fro a lower solute conc to higher solute conc and thru the semi permeable membrane which stops the solute from moving
active transport requires
energy in the form of ATP
faciliatted diffusion (passive transport)
for large,charged or polar molecules
so integral membrane proteins help faciliate the movement
endo and exocytosis
creates environments for a specific process like
endocytosis:
ingestion of material (which is kept away from cytosol because could be toxic) into cell by cellular membrane —-
pinocytosis -ingestion of fluid and small particles
phagocytosis-for larger particles
exocytosis
oppsoite of endocytosis
like in nervous system or intracellualr signalling
movement for what type of molecules
active
facilitated
osmosis
diffusion
polar charged
large,polar and charged
water
small and non polar
epithelial tissue
helps with protection from invasion or dessication
also helps with secretion,absorption or even sensation
connective tissue
provides framework like in tendons,adipose tissue ,cartilage
nervous tissue
helps with coordinated contorl,signalling using electrochemical gradient
virus
-acellular
-OBLIGATE INTRACELLULAR PARASITES—do not replicate on their own
-hijacks a cell machinery and starts producing virions
-protien coating is called capsid
what are bacteriophage
a type of virus that attacks bacterial cells
doesnt enter entirely but sends out genetic material inside for replication
diseases caused by virus are
mumps, measles,chicken pox,influenza,hepatitis ,AIDS
why is ti more difficult to treat a viral disease than a bacterial one
virus doesnt have its own organelles and lives inside host cells —so difficult to comabt eh viral replication and destroy htem using vaccination
wernicke kershakoff syndrome
balance problem,delirium and excessive alcohol consumption leading to difficulty in forming memories
characterstics of enzymes (proteins)
lowers activation energy,doesnt change equilibrium constant , increases rate of rxn, doesnt change H or G , aren’t consumed or changed in a reaction and are specific for a specific chemical(substrate)
lock and key theory
an active site of the enzyme having a specific shape for the Key(substrate -specific) to attach itself to
induced fit theory
-more scientifically proven
-based on conformational shifts made when enzymes and substrate meet at active site
and after the release —both come back to normal shape and state (shift )
-releases and absorbs energy during these conformational shifts
thiamin ?
a cofactor for enzymes that control metabolism or nerve conduction and its deficincy leads to the wernicke syndrome
cofactors are
nonprotein molecules that make enzymes efficient
types of cofactors
1.organic (co enzyme)
2.Metal ion
human cofactor name
biotin
holoenzyme and aponenzyme
enzyme with cofactor and enzyme without cofactor
factors affecting enzyme kinteics
pH, temperature,conc. of substrate / enzyme
Km is directly proptoriomnal to
affinity for the susbtrate
½ V max is
Km= S
effect of temperature
works best when risen to optimal (37 degree) and after that it becomes denatured
pepsin
works best at 2 pH
pancreatic enzymes near small intestine work at
8.5 pH
7.3 in human blood is still considered as
ACIDOSIS
allosteric effects
allosteric sites—sites other than active sites
enzymes are of two types here:
allosteric inhibitors or activators
-activators will increase the binding power of the active site for the substrate whereas inhibitor will lessen it
-other than that,affinity of an enzyme for a substrate is also affected by this
hemoglobin binded to one oxygen unit
increases affinity to bind to the other subunits of oxygen
inhibition has 3 types:
non competitive,uncompetitive and competitive
competitive inhibiton
-occupies the active site and can be removed by
addng more substrate or increasing th substrate: inhibitor ratio
noncompetitive inhibition
occupy other binding sites but not the active one (Allosteric site)
-cannot be removed by adding more substrate
-reduced the Vmax but the Km remains constant
what does non competitive mean here
the allosteric and the active sites are not competing for the same spot, and so no competition lies here
example of irreversible inhibition
aspirin (acetylsalicylic acid)—-actelyases cyclooxygenase and prevents pain
thus cyclooxygenase needs to be synthesized more using tracritpion and translation to produce prostaglandins
what does feedback inhibition effect do in general
the product is too much so it just binds to the enzyme to not be able to bind to substrate to produce more product
example of why tight control of an enzyme is required
trypsing (digestive enzyme) will digest the organ itself if not controlled
what are used to control the enzyme rates
zygomens(inactive forms of enzymes ) like trypsinogen for trypsin
zygomens have
-regulatory domain(needs to be removed before use)
-catalytic domain
what works the same as zygomens ?
apoptic enzymes
how does a person suffering from methanol poisioning treated ?
providing intravenous ethanol which works like an inactive form of the methanol
coenzyme Q10 effects
-antioxidant
-immune functions
-biochemical fucntions
-implicable in parkinson and alzeihmer
-anti aging fighting against the free radical chemicals
where is Q10 found
-inner mitochondirla membrane and helps produce ATP
plants and human ?
anabolic and catabolic (we break down organic moelcules produced by plants)
glucose configuartion is also called
pyranose (a ring structure)
photosynthesis characterstics
-endothermic
-plants are anabolic in nature
-C-O in CO2 and O-H in H2O is broken down and then rearranged to form the main mediator called glucose
ATP
made of adenine nitorgen base, ribose sugar and 3 phosphate groups
ribose and deoxyribose difference
2’C — 2’OH (ribose)
2’C——2’H (deoxy)
where is energy stored in atp and why is it called high energy ?
-high energy because 3 phoshpate groups mean too many negative charges in closer proximity to one another
-stored in 3 phoshpate bonds
ATP can be broken down to:
ADP+ inorganic phosphate
AMP + pyrophosphate
hydride ions are good?
reducing agents like LiAlH4 or NaBH4
how much energy always releases
approx 7Kcal/mol
most energy needed for muscle contraction or actvie transport is by
ATP breakdown or glucose catabolism
coenzymes are
NAD+ and FAD
coenzymes do what role?
accept high energy electrons
high energy electrons are in the form of
Hydride ions —whihc do not give away their energy but are transported
these electrons are transported to what ?
to an electron acceptor (oxygen) which couples to give ATP production
what does High energy electron do?
travels through thr ETC in inner mitochondrial matrix to be able to convert to ATp again for use
what happens to NAD+ and FAD in glycolysis and Krebs?
reduces to NADH and FADH2 (after receing electrons in the form of Hydride)
glyoclysis in short term is
breaking own gluocse to two smaller organic molecules and occurs in the cytoplasm