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85 Cards in this Set

  • Front
  • Back

Characteristics of Mitochondria


Double membrane bound organelle


Mitochondrial DNA is present


Contains large number of integral proteins


Postulated to have arisen from endosymbiosis


site of ATP production


found in nearly all eukaryotic cells


contains two membranes: cristae and matrix







Endosymbiosis

Evolutionary theory which entertains the concept that eukaryotes evolved from prokaryotes by consuming prokaryotes and they essentially live inside one another

Microtubules

made of alpha and beta tubulin monomers


thickest and form hollow tubes


involved in support, organelle transport, cell division and movement


Grows from centrosomes


constituent of cilia and flagella

Organelles for energy production



produces usable chemical energy for the cell from other sources


energy stored in chemical bonds


include mitochondria and chloroplast

Peroxisomes

Breakdown of peptide bonds in metabolism

peroxisomes

digest lipids



lysosomes

hydrolyze peptides in the cytosol


Digest worn out organelles, food particles engulfed bacteria/virus

proteosomes

hydrolyze extracellular peptides


Degrades unneeded or misfolded proteins through proteolysis, which is hydrolysis, specifically for proteins.

ATP is a result of

respiration occuring in the mitochondria

Mitochondria membranes

inner: convoluted and contains some respiratory enzymes


internal space: contains mtDNA, respiratory enzymes, and ribosomes.


high surface to volume ratio

mitochondrial matrix

found in the inner membrane


interior or mitochondria created by inner membrane

Cristae

found in the inner membranecreates the folds found within the mitochondria


contains proteins and molecules used for making chemical energy.

Endoplasmic Reticulum

network of sacs and tubules (cisternae)


continuous with the outer nuclear membrane


Interior: (cisternal space) continuous with space between nuclear membranes


smooth and rough



Smooth ER

lipid synthesis, carbohydrate metabolism, calcium storage and detoxification

rough

ribosomes on cytoplasmic face


site of protein synthesis and modification (glycoproteins)


vesicles bud and go to Golgi

Liver

Organ with a function similar to the smooth ER. Detoxifies alcohols and medicines

cytosol

fluid within the cell membrane.

Constituents Endomembrane system

Nucleus, ER, Golgi, lysosomes, vesicles

Endomembrane system with labels

Golgi apparatus

destination of most ER vesicles


modify ER products, store temporarily before sending elsewhere


synthesizes some polysaccharides



Golgi apparatus constituents

Stacked cisternae


cis: recieves ER vesicles


trans: finished products from Golgi processing


vesicles



Golgi apparatus and constituents

Functions of endoplasmic reticulum

Folds proteins molecules in cisternae


transports synthesized proteins in vesicles to the Golgi apparatus

Vesicles

small transport structure made of a phospholipid bilayer

Function of ER and Golgi apparatus

modify plasma membrane lipids and proteins


*maybe*

Lysosomes

acidic compartment (pH approximately 5) used to digest macromolecules


controls cells death (cell lysis)



what forms lysosomes

trans Golgi


phagocytosis


recycled cellular material

Proteasomes

Large protein complex


Degrades proteins into polypeptides which get recycled to amino acids



degredation of proteins control function

Mitosis


Apoptosis


Cell signaling and communication


Gene expression


Immunity

Vacuoles

important in storage and homeostasis

Central vacuole in plants

contractile and vacuole

Peroxisomes

transfer H to O2 (2H+O2-->H2O2)




important in digesting some molecules (lipids)




does not form by budding from Golgi


often cooperate with energy organelles

Chloroplast function

site of photosynthesis (conversion of light energy into chemical)


important for carb production

Chloroplast structure

double membrane with internal membranous structure (thylakoid)


thylakoids found in stroma

stroma

thylakoids found here; stroma also contains chloroplast DNA, Riboslmes and enzymes for protein synthesis.


connective tissue and structural framework of chloroplast

thylakoid

site of light dependent reactions in photosynthesis

granum

stacks of thylacoids

Endosymbiotic theory

big cell ate little cell to give rise to some organelles


proteins within made by ribosomes within organelle or by free ribosomes


grow and reproduce on own


encased in double membrane


maintain their own DNA


same size as prokaryote

Keratin

Supercoiled fibrous proteins

Free Energy

total energy + entropy


deltaG= deltaH-T*deltaS



As free energy increases stability ____

decreases

A spontaneous reaction occurs under what conditions

deltaG < 0 (releases energy)


Enthalpy decreases while entropy increases

Catabolic metabolism

Releases energy used to drive chemical reactions.


Breakdown of complex organic molecules into simpler ones


Free energy: G< 0


releases energy


Energy released supports anabolic reactions



Anabolic metabolism

Simpler substances combine to form more complex molecules


Requires input energy


Non spontaneous


G>0





Equilibrium

G=0

Chemical reactions in cells are usually

in equilibrium

Chemical reactions in equilibrium are not favorable to living organisms because

No work can be done in equilibrium reactions

Exergonic

Energy is released= catabolism

Endergonic

Energy is absorbed = anabolism

Hydolysis of Sugar

C6H12O6-> 6H2O+6CO2


deltaG= -686 kcal/mol


exergonic

Synthesis of sugar

6H2O+6CO2+light-> C6H12O6+ 6CO2


endergonic


686 kcal/mol

When deltaG is negative the reaction is considered

catabolic, exergonic

Anabolic

building up/synthesis


endergonic reactions, anabolic, requires energy

more covalent bonds =

more energy

Closed system

equilibrium

Open system

interacts with the environment


energy can be transferred

ATP

Adenosine triphosphate. Energy currency of the cell.


Adenosine, nucleotide, building, building blocks for RNA


Allows work, transport

Phosphoanhydride bonds

Produces a lot of energy, exergonic. 3 found in the bonds of ATP, allows for quick energy transfer

Reaction of ATP

ATP-->ADP+Pi

Energy of hydrolysis of ATP

G: -7.3 kcal/mol

Negative deltaG allows for

Allows for a chain of chemical reactions

Reaction coupling

Coupling endergonic and exergonic reactions to power each other.

Phosphate transfer in ATP

leads to a reactive intermediate

Free energy must be negative

for a reaction to proceed

Gamma

Bond farthest away from the ribose sugar in ATP. Extremely high energy and unstable

Phosphodiester bond

2 bonds broken in ATP. ASK DR. BARTON FOR CLARIFICATION

Cyclic nature of ATP

cellular respiration catabolic releases energy and breaks up ATP to ADP +Pi which is then recombined into ATP during anabolism

Spontaneity

Cells resist spontaneously occuring reactions by requireing activation energy

Transition state

Point in a chemical reaction in which activation energy requirement is met, allowing it to take place.

Enzymes

Lower activation energy required for a chemical reaction to take place

Enzymatic properties

Mostly proteins that decreases activation energy


IT DOES NOT CHANGE FREE ENERGY, only lowers activation energy

Active site

where a substrate reaction occurs.

Enzymes bond at the ___ to cause ___

active site to cause an induced fit. Like keys to a lock. Forms covalent bonds.

Enzymes are mostly

Proteins, but some nucleic acids

Enzyme action in hydrolysis of sucrose

1) enzyme available w/ empty active site


2) substrate binds to enzyme forming the enzyme/substrate complex


3) substrate converted to products and is released

Enzyme also ___ reactions

orients.

Amino acids

can function both as an acid or as a base.

Microenvironment

facilitates rxn, right where rxn is occuring

Rate of enzymatic activity is dependent on the

availability of the active size.

Denaturation

Occurs when anything influence the protein structure. pH, temperature, etc.

cofactors

non-protein helpers, cannot be transient of permanent. Usually metals, minerals

coenzyme

organic cofactors they are necessary rxn will not occur otherwise

Factors effecting enzyme activity

inhibitors

competitive inhibitor

competes with the enzyme for active site, which has a higher affinity that prevents the substrate from binding

noncompetitive

bonds to another region to disrupt activity