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200 Cards in this Set

  • Front
  • Back
chemical formula for glucose
c6h12o6
how are polymers formed?
via dehydration synthesis (aka condensation)

H of one monomer is bonded with the OH of another molecule

Product: water and a covalent bond
what facilitates the process of hydrolysis and dehydration synthesis?
enzymes
explain hydrolysis
a polymer is broken apart and using water, it forms 2 monomers
carbohydrates are?
sugars and polymers of sugars
monosaccharide
single sugar
two classes of monosaccharide
aldose (aldehyde)
ketose (ketone)
What are ways that sugars are classified?
# of C, Location of C doulble bond O group, Arrangement of parts about C
disaccharides are formed by what kind of bond? how does it occur?
glycosidic linkage

Monosaccharides undergoing dehydration synthesis to form a covalent bond

Water is given off
Polysaccharide
polymers of monosaccharides

formed by glycosidic linkages
Function of polysaccharides
energy storage
Give two examples of storage polysaccharides
Starch-used in plants and is a polymer of glucose

Glycogen- used in animals and is a polymer of glucose
What are the two forms of starch?
Amylose (1-4 link) and Amylopectin (1-6 link)
Give two examples of structural polysaccharides
Cellulose (1-4 link)
Chitin (has nitrogen appendage)
What is the difference between cellulose and starch?
Both have 1-4 carbon links but cellulose is beta glucose and starch is alpha glucose
alpha glucose
OH down
beta glucose
OH up
polynucleotide is synonymous with
nucleic acid
what are the two types of nucleic acids?
DNA and RNA
what is the function of polynucleotides?
Store and transmit hereditary information
What are the 3 components of a nucleotide?
1. phosphate group
2. sugar (pentose)
3. nitrogenous base
what is the difference in structure between DNA and RNA
the sugar

sugar in DNA is deoxyribose which is a ribose w/o an O on the #2 carbon

RNA has ribose
Two "families" of nitrogenous bases
pyrimidines and purines
pyrimidines
C, T, U
purines
A, G
What is the name of the covalent bond that links nucleotides?
phosphodiester bond
C binds to
G
A binds to
T
Form of the sugar phosphate backbone
5' to 3'

5' end has the phosphate group
3' end has the OH group
What is a key difference in shape between RNA and DNA
RNA is single stranded
What is a polypeptide and how does it relate to a protein?
a polypeptide is a polymer of amino acids. A protein is one or more polypeptides that are folded into a 3-d structure
Four things that all amino acids share in common
amino group (NH2)
carboxyl group (COOH)
H
terminal C with a variable group R
What are the 3 groups for amino acids
nonpolar
polar
charged
3 things that determine how amino acids are grouped
size, behavior in water, charge of side chain (r group)
What is the name of the covalent bond that is formed between amino acids?
peptide bond
Direction of polypeptides
move from the N end to the C end
4 levels of protein structure
1.Primary – amino acid sequence
2.Secondary – backbone interactions
3.Tertiary – R group interactions
4.Quaternary 2 or more polypeptides
Primary structure
protein's amino acid sequence
secondary structure
alpha helix or beta pleated
result of H bonds between N and O in the backbone
tertiary structure
interactions between R groups form the overall shape of the protein
quaternary structure
results from the aggregation of polypeptides

not all proteins do this
one thing that all lipids have in common
they are hydrophobic
what is the function of fats
energy storage, insulator, protection
structure of a fatty acid
long chain of carbon w/ one non-polar end and a carboxyl group on the other
What is the name of the bond when fats are formed and how is it formed?
ester linkage

bond between a hydroxyl group and a carboxyl group
How is a fat formed
3 fatty acids link with hydroxyl groups of a glycerol
Saturated fatty acid
no double bonds, every C bond has a H

solid at room temp

butter
unsaturated fatty acid
has double bond, not saturated w/ H

healthier

oil
phospholipids: explain their structure and why they are so essential
they make up most of our membranes

have a polar head and nonpolar tail
What is a steroid and how is it shaped?
It is a lipid

C skeleton fused with 4 rings
Organelles
tiny organs with specialized function that are bounded by membranes
cytoplasm
region between the nucelus and the plasma membrane of the eukaryotic cell

includes cytosol and organelles
cytosol
internal fluid of the cell that supports organelles

filled with ions and salts
3 components of the cytoskeleton
Microfiliaments
Intermediate filaments
Microtubules
what is the function of the nucleus?
brains of the cell where most of the DNA is kept`
What is the structure of the nucleus?
nuclear envelope
nuclear lamina
chromosomes and chromatin
What function does the pore on the nuclear envelope play?
It allows for the entry and exit of proteins, RNA, and macromolecules.

In particular, it lets out mRNA, which are coded with DNA instructions. Once in the cytoplasm, ribosomes will read them, and translate them into proteins
nuclear lamina
a net of proteins that help shape the nucleus and provide support for the envelope

these are usually intermediate filaments that are based by the protein keratin
chromatin
a complex of proteins and DNA that make up chromosomes
chromosomes
are structures that carry genetic information

vary in # from species to species
Ribosomes and their two types
make proteins

free-chill in the cytosol and make proteins that remain in the cytosol

bound- on the ER or nuclear envelope and make proteins that are to be secreted
Is the plasma membrane part of the endomembrane system?
Yes, because vesicles will connect to it to dump off proteins
lumen
cavity of the ER
Function of Smooth ER and give examples of its function
helps with metabolic processes

Sex hormones steroids
Adrenal gland steroids
Detox in the liver
Stores Ca ion to assist in muscle contraction
Function the Rough ER
protein synthesis and distribution

ribosomes dump proteins
ER adds sugars to create glycoproteins

ER separates out based on destination and are moved by transport vesicles
Golgi apparatus function and process
shipping and modification of proteins

cis-enter
+/- carbohydrates
trans-leave

also makes polysaccharides
cytoskeleton functions
shape
cell motility
anchor for organelles
trackes the movement of cell parts
cytoskeleton and cell nutrient transport
motor proteins will hold cargo and walk up and down parts of the cytoskeleton
microtubules: function, structure, protein subunit
Function: cell shape, cell motility, organelle and chromosome movement

Structure: tube

Protein: alpha and beta tubulin
Rank the size of microtubules, microfilaments, and intermediate filaments
microtubules (large)
intermediate filaments
microfilaments (smallest)
centrosome
microtubule organizing cent er in the cell that is used in replication
centrioles
are where microtubules will attach

the centrosome contains 2 centrioles

each centriole contains 9 triplet microtubules
microtubules and cell motility
found in cilia (short and many) flagella (singular w/ wave like motion)

9 + 2 arrangement forming a wagon wheel w/ assist of proteins--function is to keep it rigid
basal body
anchors flagella/cilia
explain the movement of cilia/flagella
dyenin proteins are between doublet microtubules

ATP gives energy that causes a walking motion, moving up the tube

cross linking of proteins causing a bending motion and doesn't allow the proteins to walk too far
Microfilaments: function, structure, protein subunit
Function: change in cell shape, muscle contraction, streaming and pseudopodia movement

Structure: two intertwined strands

Protein: Actin
cisternal maturation model
processing of proteins in the golgi from the cis to the trans face
microfilaments in relation to pseudopodia
provide support during movement

gel-actin in the outer cytoplasm
sol -actin in the inner cytoplasm

actin will interact with myosin and squeeze the interior which will move the cytoplasm
microfilaments in relation to cytoplasmic streaming
actin filaments that are parallel act as a "carpet" for cycling cytoplasm
microfilaments and muscle movement
myosin (thicker network of protein filaments) walk and move actin filaments closer together to maker the cell smaller --> contraction
Intermediate filament: function, shape, and protein subunit
function: tension bering, anchorage of nucleus and certain organelles, formation of nuclear lamina

structure: fibrous proteins supercoiled into thicker cables

protein subunits: keratin family
What is the function of the mitochondria
synthesizing energy (ATP)
what two organelles are double membraned?
chloroplasts and mitochondria
cristae
inner foldings of the mitochondria that give extra surface area to enhance cellular respiration

enzymes dock on the membrane
matrix
the space in the mitochondria that contains DNA and ribosomes
What is the function of the extracellular matrix in animal cells?
-frame-structural support where cells can attach
-separate different tissues in an organism
-regulate cell-cell communication
glycoprotein
proteins with covalently bonded carbohydrate, usually a short chain of sugars
What is the most abundant glycoprotein in the ECM?
collagen
What is the ECM mainly composed of?
glycoproteins
what is the function of collagen
it forms strong fibers outside of the cell
proteoglycans
network of glycoproteins that are interwoven with collagen
fibronectin
attaches the extracellular matrix to integrins that are embedded in the plasma membrane
integrins
membrane proteins that bind to the ECM and also to the microfilaments in the cell
What four things make up the structure of the ECM
collagen
proteoglycans
fibronectin
integrins
What are the three intercellular junctions
tight junctions
desmosomes
gap junctions
tight junctions
the plasma membrane of neighboring cells are tightly pressed against each other and are bound by proteins

they help to seal and prevent leakage
desmosomes
function like rivets that fasten cells together into strong sheets

-intermediate filaments assist in the process that are made of keratin

help anchor cells together
gap junctions
provide cytoplasmic channels from one cell to an adjacent cell.

allow for communication between cells
phospholipid bilayer and amphipathic
it has a hydrophilic head (polar)
and a hydrophobic tail (non polar)

reason for the assembly of the phospholipid bilayer
What are the two types of movement in the phos. bilayer
lateral movement (side to side) --frequent

flip flop --doesn't happen as often
What are three factors that affect fluidity
1. saturation
2. temperature
3. cholesterol
How does unsaturated fatty acids affect fluidity?
increase fluidity because it keeps the molecules from packing together
How does saturated fatty acids affect fluidity?
increase viscosity (less fluid) because it allows for close packing
How does cholestrol affect fluidity?
it reduces fluidity because it packs into the bilayer
What are the 4 parts that make up the fluid mosaic model?
lipid bilayer
cholestrol
carbohydrates
membrane proteins
Integral proteins
penetrate the hydrophobic core of the lipid bilayer.
Peripheral proteins
not embedded in the lipid bilayer at all

they are appendages loosely bound to the surface of the membrane
transmembrane proteins
span the membrane, being exposed to inside and out
What are some functions of membrane proteins
transport
enzymatic activity
signal transduction
cell cell recognition
intercellular joining
attaching to the ECM
What is allowed to pass through in selective permeability?
small non polar molecules
diffusion
the tendency of molecules to spread out evenly
What is the direction of movement in diffusion
from a high concentration to a low concentration
Passive transport
diffusion from high to low
doesn't require any extra energy
Facilitated transport
transport proteins help large polar molecules diffuse from high to low concentration

no energy cost

-channel proteins and carrier proteins assist
Active transport
Transport proteins move molecules against their concentration graient

require energy
osmosis
the diffusion of water across a semi permeable membrane

high to low
tonicity
the ability of a solution to cause a cell to gain or lose water
isotonic
everyone is happy- no movement
hypertonic
the solution outside the cell has more solute and so the water leaves the cell
hypotonic
the solution inside the cell has more solute so water moves in
Explain the Sodium Potassium Pump
3 Sodiums will bind to a carrier protein (in the shape that it is in, the protein likes Na)

ATP will phosphorylate, causing the protein to change shape, no longer having an affinity for Na+, so it releases them outside the cell.

Now having an affinity for K+, the protein wil take in 2 K+, which triggers the release of the phosphoryl group, causing the shape to change and the affinity for K+
What is the consequence of the sodium potassium pump
the creation of a membrane potential, or a difference in charge.

The outside is positive, the inside is less positive
Explain the proton pump in relation to co-transport
H+ ions are moved outside of the cell, with the help of ATP and a protein. This creates a voltage difference across the membrane.

Since H+ will naturall diffuse across the membrane, sucrose is moved against its concentration gradient into the cell to provide for metabolic processes
metabolism
the totality of an organisms' chemical reactions
Energy
he capacity to cause change and can be used to do work
Two forms of energy and give an example for each
Kinectic-motion
Ex: heat (thermal energy)

potential-positoin
ex: chemical energy
catabolic pathway
break down pathways

exergonic

creates energy
anabolic pathway
forms moelcules

endergonic

requires energy
1st law of thermodynamics
energy cannot be created or destroyed; it can be transferred or transformed
2nd law of thermodynamics
Every energy transfer or transformation increases the entropy (disorder) of the universe
Relate spontaneity and entropy
A spontaneous process increase entropy
Free energy
represented by G

portion of the system's energy that can perform work when temperature and pressure are uniform throughout the system

change in free energy is =

products - reactants

final - initial
Spontaneous reactions and free energy
No energy input is required

-tendency for a system with high G to go to low G

Therefore the change in G is going to be negative
Exergonic reaction
-releases free energy
-does not require energy
-spontaneous
-delta G is less than 0
-energy becomes available to do work
Endergonic reaction
-consumes free
-requires energy
-nonspontaneous
-delta G is greater than 0
-free energy becomes stored in molecules
give an example of a catabolic pathway. is it exergonic or endergonic?
Cellular respiration is exergonic
give an example of an anabolic pathway. is it exergonic or endergonic?
Photosynthesis is endergonic
What is the goal of a living cell?
not to be in equilibrium- you are dead if you achieve total equilibrium
ATP
adenosine triphosphate
What is the structure of atp
3 phosphate groups attached to ribose, which is attached to adenine
Why is atp good for providing energy
the phosphate groups that are negatively charged are forced closer together which creates greater chemical potenital energy
What process releases the energy of atp? what are the products?
Hydrolysis of ATP

Use water to break ATP into ADP and an inorganic phosphate
ATP and performing work: what types?
coupling to make exergonic reactions
transport- binding to transport proteins
mechanical- helping motor proteins move
what is activation energy
the energy required to start a reaction
what is an enzyme and how does it help with overcoming activation energy
it is a protein that acts as a catalyst

substrates will bind to the active site of an enzyme and the interactions will weaken the bonds so that there is less energy required to begin the reaction
co factor
non protein components to an enzyme
enzyme inhibitors
agents that inhibit catalysis and prevent enzymes from acting so
what is an enzyme and how does it help with overcoming activation energy
it is a protein that acts as a catalyst

substrates will bind to the active site of an enzyme and the interactions will weaken the bonds so that there is less energy required to begin the reaction
enzyme inhibitors
agents that inhibit catalysis and prevent enzymes from acting so
competetive inhibition
in site bonding of agent
co factor
non protein components to an enzyme
competetive inhibition
in site bonding of agent
non competitive inhibition
agent bonds to outside of enzyme to change its comformation
non competitive inhibition
agent bonds to outside of enzyme to change its comformation
enzyme inhibitors
agents that inhibit catalysis and prevent enzymes from acting so
allosteric regulation
way of activating or stopping enzyme activity based on the binding of a regulatory molecule

this can stop/start a chain of chemical reactions
feedback regulation
a pathway is switched off by its own product when there is too much of it and it binds to an enzyme

prevents wasting chemical resources
allosteric regulation
way of activating or stopping enzyme activity based on the binding of a regulatory molecule

this can stop/start a chain of chemical reactions
competetive inhibition
in site bonding of agent
feedback regulation
a pathway is switched off by its own product when there is too much of it and it binds to an enzyme

prevents wasting chemical resources
non competitive inhibition
agent bonds to outside of enzyme to change its comformation
allosteric regulation
way of activating or stopping enzyme activity based on the binding of a regulatory molecule

this can stop/start a chain of chemical reactions
feedback regulation
a pathway is switched off by its own product when there is too much of it and it binds to an enzyme

prevents wasting chemical resources
Oxidative phosphorylation
Energy that is released through a series of redox reactions that is stored for the creation of ATP by combining an inorganic phosphate and ADP
Substrate-level phosphorylation
A substrate containing a phosphate group binds to an enzyme, along with ADP, and the P of the substrate is transferred to the ADP --> production of ATP
Overall reaction for cellular respiration
C6H12O6 + 6O2 --> 6CO2 + 6H2O + Energy
What is the purpose of cellular respiration
to oxidize food molecules via O2 in order to make ATP to use for the body's metabolic processes
How is energy controlled in cellular respiration?
It is incrementally released through the step-wise process of breaking bonds
Where does glycolysis occur
in the cytosol
What are the three focus areas of action for cellular respiration
Glycolysis
Citric acid cycle
Oxidative phosphorylation: ETC + Chemiosmosis
How many steps is glycolysis?
10
What in essence happens during glycolysis?
it is the process of breaking glucose into a molecule that the citric acid cycle can use, which is pyruvate
Is glycolysis aerobic or anaerobic?
anaerobic (no o2)
Pyruvate contains how many C?
3
how many ATP are produced during glycolysis?
2
Summarize the energy investment phase of glycolysis
Glucose ( 6 carbon) will turn into 2 glyceraldehyde 3 phosphate ( a 3 C molecule w/ a Pi)

This requires 2 ATP and produces 2 ADP
What are the two general phases of glycolysis
energy investment -uses ATP
energy pay off - produces ATP
Summarize the energy pay off phase of glycolysis
2 of glyceraldehyde 3 phosphate are turned into 2 pyruvate molecules.

This requires 2 NAD+ which will be reduced to 2NADH + 2H+

2 Pi and 4 ADP will be required as well

It will produce 2 ATP
Where does the citric acid cycle take place
mitochondrial matrix
How many NAD+ are required for the citric acid cycle?
8
How many NADH and H+ are produced during the citric acid cycle?
8
How many ATP are produced in the citric acid cycle?
2
Why is pyruvate converted into acetyl CoA
because it is more reactive due to its greater chemical potential energy
Summarize what happens in the Citric Acid Cycle?
pyruvate is converted to acetyl coA
Requires: NAD+ and Coenzyme A
Produces: CO2 and NADH+ + H+

Acetyl co A is attached to a 4 C molecule (oxaloacetate) to make a 6C Citric Acid molecule

Electrons are stripped by NAD+ leading to the oxidation of C

2 CO2 are released

1 ATP is generated

The 4 C molecule (oxaloacetate) is regenerated
Requires: FAD --> FADH2
NAD+ --> NADH+ + H+
acetyl coA has how many carbons?
2
How many electrons are transferred in the citric acid cycle?
20 overall
How many times does the citric acid cycle occur?
twice to accomodate the 2 pyruvate
Oxidative Phosphorylation creates ATP how?
via redox reactions that phosphorylated ADP
Where is the ETC located?
inner mitochondrial matrix
what is the structure of the ETC
carrier proteins are bound w/ cofactors in order to form complexes

3 are embedded into the membrane
2 are mobile
How does the ETC work?
NADH and FADH2 are oxidized and the electrons are passed down their energy gradient down the electron acceptors, releasing energy progressively, until the last set of electrons reach Oxygen

During this process hydrogen ions are pumped across the membrane

this leads to a product of water
atp synthase
the enzyme that makes ATP from ADP and Pi with the help of a proton gradient
How does chemiosmosis work
H+ move with their concentration gradient and bind into the rotor of atp synthase which then causes it to rotate which catalyzes the production of ATP
How many net ATP are made at the end of cellular respiration
38 or 36 ATP
What is fermentation
it is an extension of glycolysis that has an extra step to recycle NADH back to NAD

uses substrate phosphorylation

generates ATP with out oxygen
Alcohol fermentation
turns pyruvate into ethanol

1. Co2 released to turn 3 C pyruvate into a 2C molecule

2. the 2C molecule turns into ethanol by the reduction of NADH to NAD
What is the use of alcoholic fermentation?
yeast for bread
sugar for beverages
Lactic acid fermentation
pyruvate is directly converted into lactate by being reduced by NADH
uses for lactic acid fermentation
cheese

animal muscle cells in exercise
Why is NAD+ a good oxidizing agent?
Because electrons lose very little of their potential energy when they are transferred from glucose.

The chemical bonds are good storage for potential energy