CHNOPS
carbonhydrogennitrogenoxygenphopshatesulfur
What are the four major classes of biomolecules
proteinsnucleic acidslipidscarbs
What is CHNOPS
the atoms that are present in biomolecules
what are the three atoms that are major elements of the human body
hydrogenoxygencarbon
covalent bonds
shared electron pair btw two atoms
non-covalent bonds
Hydrogen bondsVan der waals Ionic Bonds
what are proteins made up of
20 amino acids
how do amino acids form polymers
they are linked by peptide bonds
amino acid polymers______
fold into precise secondary and tertiary structures to form a protein
Nucleosides
adenine (a)cytosine (c)guanine (g)thymine (t)
nucelotides
nucleosides with phosphate group added
deoxyribonucleic acid (DNA)
-2x helix-linked by phosphodiester bond
ribonucleic acid (RNA)
-single stranded-transcribed from DNA-gets translated into protein
lipids function
lies with dual nature hydrophobic and hydrophilic parts
lipids are critical ___ and are a form___
in the formation of cell membranes-energy
carbs are____ and its most common form is
fuel sources for cellsglucose
glucose is stored as___ and it plays a role in____
as glycogencell- cell recognition and interaction
The Central Dogma
DNA-transcription-RNA-translation-protein
Prokaryotic cells
-no nucleus -genetic info is free floating in cytoplasm as single strand of dna
Eukaryotic cells
-membrane bound organells-lots of genetic Information in nucleus
Membranes are a ____
lipid bilayer
difference in Eukaryotic and prokaryotic membrane
eukaryotic cells contain membrane enclosed compartments
similarities in eukaryotic and prokaryotic membranes
both have plasma membrane
the plasma membrane
protects the cell from the outside environment
Where is the cytoplasm located?
in the plasma membrane
The plasma membrane is _____ to most substances, but it is____
impermeable selectively permeability
selective permeabiliity
allowed by membrane proteins that facilitate the entrance and exit of critical molecules for the cell
the cytoplasm is the
site of many biochemical processes such as glucose metabolism, fatty acid synthesis and protein synthesis
how is the cytoplasm organized
cellular cytoskeleton
biochemical reactions are____
sequestered into cellular compartments called organelles
Nucleus
-largest organelle-double membrane bound-where cells entire genome is found
The pores in the nucleus allows for what
protein transport in and out of the nucleus
The nucleus regulates genomic information by
expressing the information at the correct tome and in the correct amount
mitochondria
-powerhouse of the cell-contains two membranes
inter membrane space
the space between the mitochondrial two membranes
how much of the cells energy is produced in the mitochondria
90%
what is the main source of energy produced in the mitochondria and how is it made
ATP and oxidative phosphorylation
Smooth ER
processes extracellular chemicals
Rough ER
appears rough due to the ribosomes attached
chaperons
take the proteins that are synthesized in the er to the lumen where folding occurs
transport vessicles
allow for folded modified and finalized proteins to leave the lumen
ribosomes are responsible for
the translation of RNA to proteins
After the proteins leave the rough ER, they move to the_____ to be sorted
Golgi complex
proteins in the Golgi that have been tagged for secretion will be contained by
secretory vesicles
secretory vesicles Duse with the plasma membrane and the contents get released with the correct signals. this process is called ---
EXOCYTOSIS
Endosomes
vesicles formed when cells take up material through endocytosis
phagocytosis
when large amounts are taken up by the cell
Lysosomes
organelles that contain a wide array of digestive enzymes
____ AND _____ fuse together in order to digest the engulfed material
lysosomes and endosomes
Lysosomes also digest
damaged intracellular organelles
Overview of cellular metabolism
-cell need energy-energy is the capacity to work-energy is stored in chemical bonds-energy is used to form chemical bonds and released when breaking them
Anabolic metabolism
the buildingrequires energy
catabolic metabolism
degrading of largersome energy release
ATP
the most abundant energy carrier molecule in the cells
proteomics
the field of study that isolates and analyzes protein structure and full range of functions
What are the 4 different groups that are attached to the central carbon
hydrogen atombasic amino groupacidic carboxyl groupside chain
Because all amino acids contain one asymmetric carbo atom, there are ___ isomers formed called ___ and ___
2dl
all amino acids in proteins are in the ___ conformation
l
What decides amino acid properties
the side chain
hydrophilic (polar) side chains
exposed on the surface of the protein
hydrophobic (non polar) side chains
buried in the interior of the protein
Amino acids are____ meaning they have ___ and ___ groups
amphoteric basic acidic
At pH 7. the ______ is the dominant species
zwitterion
at acidic ph, amino acids are protonated forming the____. at basic ph, amino acids produce ____
cationanion
the overall charge of a protein depends on ____
the contribution form basic (+) and acidic (-) amino acids
charge varies with
pH of solution the molecule is in
The Henderson-hasselbalch equation
describes the titration of an amino acid and can be used to predict the net charge and isoelectric point of protein
Ka
the dissociation constant of a weak acid
The Henderson hasselbalch equation can determine
the acid base equilibrium of systems
The Henderson hasselbalch equation is useful in demonstrating
the net charge of an amino will vary with the pKa of the functional groups and the ph of solution
pKa
the point when the acidic and basic forms are in equilibrium
buffers
solutions that minimize pH (change in H+)
buffers consist of
a weak acid or base and its counter ion
when does the maximal buffering capacity occurs
at the molecules pKa
why are amino acids and proteins are excellent buffers
-the amphoteric nature-the basic and acidic components have their own pKa
isoelectric point
the point between the separate pKa values of an amino acid in the solution
buffering capacity is the weakest at the
isoelectric point
Why do we care about pH??
drastic changes in pH can alter the form pf proteins and enzymes and prevent chemical reactions from taking place
what are the three buffer systems in body
bicarbonate bufferprotein buffer (hemoglobin)phosphate buffer
bicarbonate buffer
very important blood buffer
protein buffer systems
-donate or accept protons-powerful buffers
phosphate buffer systems
-weak acid-conjugate base pair-have pKa 7.2
the primary structure of proteins
the linear sequence of a proteins amino acids
Amino acids are linked
from N terminus (amino group) to C terminus (carboxyl group)
residue
each amino acid in a peptide chain
the sequence of amino acids are always written
left to rightn to c terminus
What determines the structure and function of a protein
its amino acid sequence
----- plays a large role in protein folding.
hydrophobicity
entropy
a measure of randomness
the hydrophobic effect
an entropy driven association btw molecules
Entropy of water molecules_____ when around non polar molecules
decrease
When the entropy of water molecules decrease, it drives non polar molecules to one another causing entropy to ___
increase
hydrophobic interactions
form spontaneously (no energy required) because they increase the entropy of water
Many____ bonds like ____ and ____ form in the folding process to stabilize the 3d structure
weakhydrogenvan der Waals
How is the secondary structure of proteins determined
by hydrogen bond interactions btw backbone carbonyl and amide groups
what are the three types of secondary structures
- alpha helices-beta sheetsreverse turns and loops
alpha helix
a rod like structure in which the polypeptide chain is tightly coiled and amino side chains extend outward
in the alpha helix, each amino acid is_____ to another amino acid that is ____ residues away
hydrogen bonded4
what direction does an alpha helix wind
right handed turns
B pleated sheets
when hydrogen bonds are formed laterally between peptide bonds, polypeptides align parallel or anti-parallel to one another
proteins have ____ shapes that require requires direction reversals in the polypeptide chain called___ and ___
globular reverse turns and loops
where are reverse loops and turns found within the protein and why
on the surface so that they interact with other proteins and the environment
loops are composed of amino acids with____ groups because they are exposed to an ____ environment
hydrophilicaqueous
tertiary structure of proteins
determined by interactions btw side chain functional groups
what all is include in tertiary structure
disulfide bondshydrogen bindssalt bridgeshydrophobic interactions
what does the tertiary structure of a protein define
a fully folded and functional protein
tertiary and secondary structures of a protein can be unfolded/destroyed by ___
denaturants or chaotropic agents
globular proteins
have a compact 3d structure and are water soulableperform most of the chemical transactions in the cell
myoglobin is a globular protein with only ____ interior residues, which binds with ___ and ___
2 polarheme iron and oxygen
the outside of myoglobin consists of
polar and non polar residues that interact with water making it soluble
van der Waals interaction contribute to
the stability of tertiary structure of proteins
protein structure =
function
motifs
combos of secondary structures that exhibit similar functions
an example of a motif
helix- turn- helix which are found in many proteins that bind with DNA
Domains
two or more compact regions that many be connected by a flexible segment or polypeptide chain
different proteins can have domains in common even if
their overall tertiary structure are different
Quaternary structure of proteins
define the combo of two or more tertiary structures to form a multi-subunit protein
In quaternary structures, each subunit can
have the the identical function or a completely separate function
dimer
the simplest quaternary structure (two subunits)
what are are the four things that protein purification is based on?
size, charge, solubility, ligand binding
why do proteins require purification?
to determine its primary, secondary, and tertiary structure
purification
the separation of the protein of interest form complex biological mixtures (cells, blood, tissue)
what must happen to cells to remove the protein?
they must. be broken open to release their content
homogenate
a mixture of all components of the cell but not intact cells
Supernatant
The (usually) clear liquid left behind after a precipitate has been spun down to the bottom of a vessel by centrifugation
differential centrifugation
the multiple centrifugation steps that provide supernatants of varying densities
crude extract
supernatant used for extraction of the protein
Proteins can be precipitated by change the salt [x] of the solution. What happens when you increase and decrease the salt [x]?
increase= more soluble decrease= less soluble
Protein precipitation may also occur when ______
adjusting pH
How are small molecules (salt) that are used for precipitation removed from protein solutions?
dialysis and ultrafiltration
What is a dialysis membrane and how is it used?
a membrane that has a molecular weight cut off (MWCO) meaning that molecules that are at or smaller than that molecular weight can pass through the membrane, where as proteins will remain separated inside of the membrane
Ultrafiltration
uses the same process but adds pressure to the technique to force a solution thru a membrane
How does cel filtration chromatography separate proteins
on the basis of size
Gel filtration utilizes ____ to separate proteins
column of highly. hydrated polymers
what is the principle of gel filtration
its is based upon the differential migration of dissolved solutes through gels that have pores of defined sizes
gel filtration is _____ for protein purification and desalting
frequently used
What happens with the protein during ion-exchange chromatography?
proteins will bind to ion exchange matrices based on the charge to charge interactions
Proteins can be separated during ion-exchange chromatography based upon
on the basis of their bet charge
If the immobilized phase is positively charged during ion exchange chromatography and if its negative?
positive= anion exchange columnnegative= cation exchange column
elution
positively charged proteins can be removed from an ion exchange column by increasing the salt [x] of the buffer poured over the column
affinity chromatography
purifies proteins based on ligand interactions
What characteristic does affinity chromatography take advantage of when purifying proteins?
the fact that some proteins have a high affinity for specific chemical groups or molecules
High-pressure liquid chromatography (HPLC)
is an enchanted version of the column techniques for purifying proteins that have already been discussed
the resolving power of HLPC
is the ability of a column to separate individual proteins
____ must be applied to the column during HLPC so that it is able to have adequate flow rates
pressure
What does HLPC result in
high resolution and rapid separation
What is gel electrophoresis?
the action of a molecule with a net charge moving in an electric field that allows for the visualization of proteins
the distance and speed the protein moves at during electrophoresis depends on what three things
electric field strengthnet charge of protein shape of protein
What happens to large and small molecules during gel electrophoresis
large- move slowly/ stay at the top of gelsmall- move quickly/ moves thru the gel towards the bottom
how is the pH adjusted during electrophoresis
ph is adjusted so that all proteins are negatively charged
During gel electrophoresis, proteins can be separated largely by size alone with the addition of the detergent_____
sds page
what does SDS do ?
binds denatured proteins at a ration of one SDS molecule per every two amino acid which gives all proteins the same charge to mass ratio
How are proteins separated during isoelectric focusing
they are separated electrophoretically based on their relative contents of acidic and basic residues
isoelectric point (pI)
the pH of a protein at which its net charge is zero
how sensitive is isoelectric focusing?
it is able to separate proteins differing by one net charge
two-dimensional electrophoresis
isoelectric focusing (1st step) combined with SDS-PAGE(second step)
what is two-dimensional electrophoresis normally coupled with and why?
mass spectroscopy to identify the protein responsible for each spot on the gel
What must happen to a protein before the primary structure analysis occurs?
the protein must be purified from contaminating proteins
how is the purity of a protein monitored
by SDS-PAGE
To determine the primary structure of a protein, what must happen
both sequence analysis and protein identification for primary structure is done by mass spectroscopy
Primary sequence info is critical for understanding the____ and therefore the_____
protein structure and function
Edman Degradation
removes one residue at a time form the N terminal end of a peptide and labels each removed residue then identifies by HLPC
Mass Spectroscopy
powerful technique that can be used to determine a protein's mass, identity, and sequence
how are mass measurements during mass spectroscopy obtained
they are obtained by determining how readily an ion accelerate through an electric field
What happens during MALDI-TOF
1. a protein is mixed with metrix2. a flash of laser expels molecules form the surface 3. the molecules capture electrons and become negatively charged
what does the TOF stand for in MALDI-TOF
the ions are accelerated toward a detector
How is protein identification accomplished during MALDI-TOF
Through the analysis of the whole protein in addition to cleaved fragments
How is the protein sequence determined during MALDI-TOF
through tandem mass spectroscopy
What is used to determine the 3D structure of proteins
x-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy
X-ray crystallography
depends on the diffraction of x-rays by the electrons of the atoms constituting the molecule
NMR
technique used for the determination of structure of a protein in a solution that complements x ray crystallography information
____ and ____ are major sources of energy
carbs and lipids
____ are hydrophilic meaning they are ___ in water, whereas ____ are hydrophobic meaning they are____ in water
carbs and soluble lipids and insoluble
carbs and lipids can both______ and play ____ and _____ functions
bind to proteinsstructural and regulatory
_____ are the simplest carb. What are their functions?
monosaccharides-serve as fuel molecules and functioning cellular components
Monosaccharides are____ or ____ that have _____ hydroxyl groups
aldehydes or ketones2 or more
____ contain keto groups and _____ contain aldehyde group
ketoses and aldoses
What are the six common Monosaccharides
D-ribose, D-deoxyribose, D-glucose, D-mannose, D-galactose, and D-fructose
What role does D-ribose and D-deoxyribose play?
components of DNA
D-glucose, D-mannose, D-galactose
abundant six-carbon aldoses
D-fructose
most abundant ketohexose
ketoses have____ than aldoses with the same number of carbons
have one less asymmetric center
The predominant forms of ribose, glucose, fructose, and many other sugars____
cyclize into rings
When does the cyclization of sugars occur
when an aldehyde reacts with an alcohol r form a Hemiacetal
In aldohexoses ( glucose) during the cyclization
the same molecule provided both the aldehyde and alcohol
Pyranose rings
hexameter rings that has c-1 as the anomeric carbon atom
Ketones react with an alcohol to form ____. what is an example?
hemiketalfructose
furganose rings
pentamer rings with c2 as the anomeric carbon atom
What are three common monosaccharide reactants
alcohols, amines, and phosphates
O-glycosidic bond
a bond formed between the anomeric carbon atom of glucose and the oxygen atom of an alcohol
glycoside
the product formed during the formation of glycosidic bond
When are O-glycosidic bonds prominent?
when carbs are linked together to form long polymers and when they are attached to proteins
N-glycosidic bond
formed when the anomeric carbon of a sugar is linked to the nitrogen atom of an amine
carbs can also form _____ to phosphates
ester linkage
Sugars contain many ____ groups allowing _____ bonds to join one monosaccharide to another
hydroxyl and glycosidic
Oligosaccharides
formed by the linkage of two or more monosaccharides by O-glycosidic bonds
Maltose
a disaccaride linked by glycosidic bind
glycosyltransferases
enzymes that catalyze the formation of glycosidic binds and are responsible for the oligosaccharide formation
Disaccharides
two sugars joined by an o-glycosidic bond
What are three common disaccharides
sucrose, lactose, maltose
sucrose is cleaved by ____. lactose is cleaved by____. maltose is cleaved by____
sucraselactasemaltase
The cleavage products of disaccharides can be further processed to form_____
ATP
___ and ___ are ___ that plat a vital role in energy storage and structural integrity of organisms
glycogen and starch polysaccharides
Homopolymer
if all of the monosaccharides in the polysaccharide are the same
what is an example of an homopolymer? What is it?
glycogen and the storage form of glucose
what is the plant version of glycogen? what are its two forms> how's is it hydrolyzed ?
starchamylose and amylopectin alpha- amylase
cellulose
a major polysaccharide pf glucose found in plants
What allows for cellulose to form very long and straight chains
the glycosidic linkages
____ and ___ produce a hollow helix
glycogen and starch
glycoproteins
carbs covalently attached to a protein
What are the three classes of glycoproteins
1. Glycoproteins- protein is the largest2. Proteoglycans- mainly carb3. Mucins- mainly carb
When a sugar attaches to an amino acid, what happens
glycosylation
What are the two linkages formed during glycosylation and where are they formed
amide nitrogen atom (N-linkage)hydroxyl oxygen atom (O-linkage)
N-linked oligosaccharides all have a common _____ core consisting of _____ and ______
pentasacchraridethree mannoses two N-acetylglucosamines
____ can be added to the common core of N linked oligosaccharides. What does this due to the molecule?
addition sugars and it forms great variety
What is an example of a glycoprotein?
erythropoietin (EPO)
lipids functions
used to store energykey components of membranesplay role sin signal-transduction pathways
lipids _______ form polymers
do not
What are the five classes of lipids
free fatty acids, triacylglycerols, phospholipids, glycolipids, steroids
what is the most common steroid
cholesterol
Fatty Acids (FA)
chains of hydrogen bearing carbon atoms called hydrocarbons
hydrocarbon chains
vary in lengths and may have one or more double bond in them
FA are ____ because the reduce more than carbs yielding____ than carbs
good fuels more energy
saturated FAs
Fas composed of single bonds only
notation 18:0 indicated____, whereas 18:2 means
C18 fatty acid with no 2x bondsc18 with 2 2x bonds
what are carbons atom 2 and 3 called and what is the last carbon refereed to ?
2= alpha3= betalast= w-carbon
FAs are ionized at
physiological pH
FAs in biological system contain
an even number of carbon atoms
the configuration of 2x bonds in the most unsaturated FAs is ____
cis
How are the 2x bonds in a polyunsaturated FAs separated by
they are separated by at least one methylene group
what do properties of FAs and the lipids made from them depend on
the chain length and the degree of saturation
What does the presence of a cis 2x bind introduce to FAs and what does this cause ?
forms a kink in the FA that makes tight packing between chains impossible which lowers its melting temp
_____ of FAs are key elements in the control of the_____ of cell membranes
melting tempsfluidity
_____ is essential for the membrane function
fluidity
what two characteristics enhance the fluidity of FAs and their derivates
short chain length cis unsaturation
What types of fats in the diet can lead to high blood levels of cholesterol and cardiovascular diseases
saturated and trans-unsaturated fats
trans unsaturated fatty acids
trigger inflammatory pathways
what types of fatty acids are essential to have in our diets because we cannot synthesize them
cis-polyunsaturate
what are some examples of cis-polyunsaturated fatty acids
w-3 fatty acids (cold water fish)alpha-linolenate (vegetable oils)etcosapentaenote and docosahexaenotae (fatty fish and shellfish)
Why are polyunsaturated fatty acids essential ?
they are precursors for important hormones
Triacygylcerols
formed by the attachment of three FA chains to a glycerol molecule via ester linkages
esterification
the Linkage of FAs to glycerol via ester linkages
What happens to triacylglycerols when energy is required
FAs are cleaved form it and carried in the cells
anhydrous
without water
Why are glycerols the major energy reservoir compared to glycogen
glycerols are anhydrous meaning that they do. not hold water so they are able to store 6x more energy than the same amount of carbs
adipose tissue
the site of accumulation of triacylglycerols
What do triacylglycerols within a fat cell
the droplets coalesce to form a large globule in the cytoplasm
adipose tissue are specialized for
the synthesis and storage of triacylglycerol and their mobilization unto fuel molecules once transported to other tissue
____ also serves as a thermal insulator
adipose tissue
What are the three major kinda of membrane lipids
phospholipidsglycolipidscholesterol
What are the four components of a phospholipid
1. one or more FAs2. a platform to which the FAs are attached 3. phosphate4. an alcohol attached to the phosphate
what are the two platforms for phospholipids
glycerol and sphingosine
Phosphoglycerides
phospholipids derived from glycerol
Phosphatidate
simplest phosphoglyceride that is a key intermediate in the biosynthesis of others and triacylglycerols
Spingolipids
phospholipids built on a sphingosine backbone
sphingosine
an amino alcohol that contains a long, unsaturated hydrocarbon chain
Sphinomyelin
common sphingolipid found in membranes
Glycolipids are_____. they are _____ in all cell membranes and are derived form____
sugar containing lipidsubiquitous sphingosine
Steroids____. They facilitate the digestion of____ in the diet. They are key_____ constitutes
are powerful hormoneslipidsmembrane
Steroids exhibit _____ rather than linear structure which leaves them with ______
cyclical steroid nucleus
steroid nucleus
consist of three cyclohexane rings and one cyclopentane ring joined together
All biochemically important steroids are modified versions of the______ structure
steroid nucleus
cholesterol is in the class of molecules called ____ which means it is a steroid with an _____ functional group
sterol alcohol
Cholesterol is found in ____ animal membranes
all
____ cholesterol does not exists outside of the membrane. Why is that?
freeit is esterified to a FA for storage and transport
Membrane lipids are amphipathic which means
they have hydrophilic and hydrophobic moiety
Hydrophobic part of membrane lipids
two fatty acid chains that run parallel to each other
hydrophilic part of membrane lipids
phosphorylcholine head points in opposite direction
shorthand of membrane lipid
hydrophilic (polar) circle headhydrophobic (non polar) tails
What happens when a lipid attaches to the protein
this allows proteins to associate with the hydrophobic environment within the membrane
How do cell membranes act like a barrier
they separate cellular interior and outside environmentthey compartmentalize organelles form cytoplasm
What are the 7 key aspects of a cell membrane
1. contains lipids, proteins, and carbs2. hydrophobic and hydrophilic 3. specialized protein families4. held together noncovalently 5. asymmetric6. fluidity7. electrically polarized
the bilayer membrane is ____
amphipathic (hydrophilic and phobic parts)
what are the two major bilayer lipids
phospholipids a nd glycolipids
hydrophobic effect
the major driving force of membrane bilayer formation
what does the permeability of small. molecules depend on
the solubility in h20 and non polar solvents
bilayers are highly
impermeable
______ content of bilayers control fluidity
fatty acids
what regulates the fluidity from rigid to fluid in bilayers
temperature
_____ also interferes with tight packing which increases the fluidity and lowers the Tm
cholesterol
____ carry out nearly ALL of membrane functions
proteins
integral membrane proteins
proteins imbedded in the hydrocarbon chains of membrane lipids that normally span bilayer
perphial membrane proteins
bound to the head groups by electrostatic or hydrogen bonds or can bind to exposed integral proteins
____ are commonly used motifs for proteins that span membranes
alpha helices
_____ are typically used to form hollow tubes to form pores or channels
beta sheets
proteins can also be embedded ____ into the membrane
partial
fluid mosaic model
basis of membrane protein motility by defining the membrane
according to the fluid mosaic model, define the membrane and lipid portions of the cell membrane
membrane= 2d structure with oriented lipids and globular proteinslipids= permeability barrier fro integral membrane proteins
Membrane proteins and lipids are in constant motion what is this motion called
lateral diffusion
lateral diffusion was discovered by _____
FRAP
how does FRAP work
A fluorescent marker is bound to the phospholipids that make up a cell membrane.Next, a laser is used to bleach a small patch of membrane (stop the patch from fluorescing) Within seconds, patch will again show fluorescence due to dispersion of phospholipids throughout the membrane meaning that there is lateral diffusion
transverse diffusion
flip flop, very slow
bilayers are____ whereas biomembranes are____
mostly impermeablenot impermeable
Intergral (transmembrane) proteins
play important roles in transporting molecules thru the membrane and often maintain molecule and ion [x] gradients
the maintenance of [x] gradients requires ____
the usage of ATP
What are the two classes of membrane transporters
channels and pumps
what are the two factors that determine molecular movement across the membrane
[x] gradient and molecular solubility
lipophilic (lipid loving) molecules pass ___ through the membrane via _____
freelysimple diffusion
polar molecules need help from ____ and ____ to get through the membrane via a process called ____
channels and porespassive transport
If a molecule must go against a [x] gradient , a ____ is needed to preform ____
pumpactive transport
Na/K ATPase pump generates ____
na/k gradients in the cell
what are the three things that Na/K ATPase pump controls
cell volume, membrane potential, and drives transports
secondary transporters
uphill movement of one molecule coupled to downhill movement of another
two types of secondary transporters
antiporters and symporters
antiporters
downhill movement drives uphill movement of another molecule
symporter
movement down a gradient used to drive movement of another molecule of the same direction
what is an example of a molecule that uses a symporter and what is it called
glucose sodium-glucose linked transporter (SGLT)
Ion transporters are rapid like_____ and are very ____ and ___ to their environment
free diffusion specific and sensitive
two examples of ion transporters
voltage gated channelsligand gated channels
voltage gated channels
opened in response to membrane potential changes
ligand gated channels
open in response to binding to small molecule