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109 Cards in this Set

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Show the balance equation for an exergonic catabolic reaction for the breakdown of sugar
C6H1206 + 602 ----> 6C02 + 6H20
Endergonic process of photosynthesis
6C02 + 6H20 -->C6H1206 + 602
686 kcal/mol
About how many membrane proteins?
no more than 25
How much of a cell is made of protein?
90% of the cell
What is Kinetics
How fast things occur
What are catalysts?
Compounds that increase the rate of reaction, but are not consume during a reaction
True or False
All bio catlysts are proteins and these are known as enzyme.
False, in 2000 we know some RNA can act as catalysts - Ribozymes (T.Czech)
How do catalysts increase rate of reaction?
molecules go through the transition state (rotational, vibration).
Does enzyme change thermodynamic of the process?
T or F
enzyme can make reaction reversible irreversible vic versa?
transfer phosphate groups to proteins
hydrolyze nucliec acids
hydrolyze proteins
catalyze oxidation reduction reactions
catalyze electron transfer H+ transfer reactions
hydrolyze ATP
How do enzyme work?
tend to be specific. If it hydrolyze one thing it probably won't hydrolize another compound
what is substrate binding site?
active site
What happens at active site?
bond in moelcule are being weakened (stretch twisted) at this transition state.
T or F
Enzyme cannot be used over and over again?
T or F
binding substrate and the release product has to be rapid?
T or F
Binding substrate has to be tightly bound?
Lock and Key model?
base on the idea that you have a lock
Induced fig model
this is moreflexible.
What is an important feature of enzyme?
Very efficient as a catalysts.
Prosthetic Groups
organic or inorganic molecules that are attach to enzyme that helps it work
ex. hemoglob. hem is prostehic
Vitamins are? And what is its function?
Co enzymes. modified vitamins inserted into protein into prostehtic groups
T or F
Trace metals are covalently bound?`
False they are not. metal ions
What other group fall in prosthetic group class?
Trace Metals. Presence as ions. Iron in heme also in non-heme.
How is Biotin attached to a protein?
Through a carboxy group.
What does Biotin do?
Involve with enzyme that take Cl2 and put it somewhere. bound at the active site of the enzyme.
What makes metal ions unique?
Very unusual feature.
What are two things that can affect enzyme activity?
Temperature and pH
Competitive inhibitors
compete with substrate (where binds at the active site of the enzyme) No or little product formation. But more substrate can overcome this. One way is to increase substrate concentration
Non-competitive inhibitors
do not bind at the active site. not affected by increase substrate concentration. Distorts enzyme and thereby decreasing likelihood of substrate binding.
What cooperativity in enzyme activity?
multiple substrate binding sites
Wehre is cooperativity generally located?
Different subunit of a protein
Where do Allosteric enzymes bind?
bind at sites other than active sites
Allosteric inhibition
binding of an allosteric inhibitor stabilizes to low affinity form
Allosteric activation
binding of this allosteric activator will stabilize enzyme in high affinity form. lots of product.
T or F
Allosteric is a substrate
What is allosteric enzyme consist of?
one or more catalystic subunits (C) and one or more regulartory subunits (R). each with allosteric and active site respectively.
What is Post-translational modification?
It occurs during the process of synth of proteins.
What is translation?
mRNA is read and the protein is made by putting amnio acid next to each other.
addition of sugar groups in Rough ER. inolve in targeting
Proteolytic cleavage is 2nd method. cleaving the polypeptide allows the fragments to fold into different shapes.
additon of phosphate alters shape of protein.
protein kinase
adds phosphate
protein phosphate
remove phosphate
What is the general idea of adding phosphate group to inactive protein
Go from totally inactive. put a phosphate it becomes totally active. Generally all or none. 0-100% activity
what makes us different than a chimp?
Two basic reasons:
1. every cell has the same dna, but not all dna are expressed.
2.assume cells have same protein not all are active
Hydrolyzes of ATP releases how much energy?
-7.3 kcal/mol
ATP lsoing terminal phophate leaving ADP and pi. what is pi
inorganic phosphate
High energy phosphate bond is a misleading term
When you hydrolyze ADP what do you get?
forms AMP and pi. free energy is -7.3 kcal/mol b/c it is a phosodiester bond.
How about hydrolyzing AMP?
adenonsine and pi. -3.5 kcal/mol b/c phosoester bond.
Know this structure. fig 101. Know how it works.
T or F
NADH reduced form?
NAD+ to NADH. How many protons and eledtrons
2 electrons 1 proton.
What is different about NADP+
has phosphate group
Oxidative phosphorylation
CO2 as prodcut, requires O2. respiration
incomplete oxidation of glucose. anaerobic process no O2 required
use oxygen
does not use oxygen
4 things
Chemiosmotic for mitochondira
1. membrane is impermeable to H+
2. electron tranpsot generates a proton gradient
3. protein gradient is an energy source
4. enzyme in membrane can convert H+ tinto ATP
List the things that you gain from glycolysis
2 pyruvate
List the things that you gain from the Kreb cycle
2 CO2

Note: when using whole glucose make sure you multiply by 2
1 NADH makes how many ATPs?
1 FADH2 makes how many ATPs?
When pyruvate converts to CoA list the products that come out
2 CO2
What is Chemiosmosis?
energy coupling mech that uses a proton gradient to drive cellular work
Regarding with fermentation
what is obligate?
requires with oxygen or without
regarding with fermentaiton
what is facultative?
can be in the presence of oxygen or without
do all photosynthetic organism have chloroplast?
No, but need light absorbing pigment
Where does the calvin cycle occur?
In the stroma
Rubisco accepts CO2 and O2. What happens when it accepts O2
it forms unuseful product for calvin cycle.
No G3P
What is the primary structure?
amino acid sequence
Secondary stucture?
folds of polypeptide into alpha helix and beta sheets.
done through hydrogen bonding
tertiary structure?
3D folding of polypeptide through disulfide bonds, hydrogen bonding, ionic, hydrophobic, and van-der-walls.
Quartenary strucutre?
same as tertiary except with polypeptide and other subunits
what happens if a protein is denature?
the 2nd, 3rd, 4th structure
glucose and glucose 1,4
galatose and glucose 1,4
fructose and glucose 1,2
short chain of polysaccarides
starch - amylose
unbranched alpha glucose
starch - amylopectin
branched alpha glucose
heavily branched alpha glucose
beta glucose unbranched
base and pentose
what are the bases for DNA?
Adenine, Guanine, Thymine, and Cytosine
What are the bases for RNA?
Adenine, Uracil, Cytosine, and Guanine
T or F
DNA and RNA are the only nucleotides
False, ATP is a nucleotide
have hydrophilic and hydrophobic regions
plasma membrane
selective barrier that regulates a cells chemical composition
Fluid mosaic model
plasma membrane is a fluid with various proteins embedded or attached
steriod a type of lipid
How does cholestrol affect the plasma membrane?
reduces fluidity at moderate Temp, but disrupts packing/solidify at low temp
cytosol and organelles
made of rRNA and proteins
not membrane bound
they make proteins
What is in the endomembrane system?
Golgi body
endoplasmic reticulum
plasma membrane
Rough ER
has bound ribosomes
makes membrane and proteins
smooth ER
synth lipids
help metab carbs
detoxify by adding -OH group
Golgi Body
modify proteins
produces polysaccarides
have hydrolytic enzymes
pH around 5
function optimally at low pH so won't denature in cytosol
stores food and waste
Mitochondria and Chloroplast
have their own DNA and ribosomes
Endosymbiotic theory
chlorplasts and mito were once prokaryotes "swallowed" by larger cell
oxidizes molecules
detoxify alcohol
their protein and lipid made from ER
not in endomembrane