Glycolysis:
2 NADH, 2 ATP, 2 NADH
TCA
6 NADH, 2 FADH2, 2 ATP
ETC/OXPHOS:
Lots of ATP
Give this one a try later!
, Cellular Respiration: Energy output per glucose
Structures of oxygenated (R state) and de-oxygenated (T state) hemoglobin differ.
The T state, or the de-oxygenated form of hemoglobin, is more stable in the absence
of O2 because of several key interactions (including ion pairs) that do not exist in the
R state.
However, when deoxy-hemoglobin binds O2, it undergoes a conformational change
that breaks many of these interactions. O2 pulls iron into the heme plane, which drags
His-F8, and the rest of the molecule, with it, giving the R state, or the oxygenated
form of hemoglobin that has a higher affinity for other O2 molecules. After the initial
bind, the second, third, and fourth O2 molecules bind at lower partial pressure
increments!
*The fact that the two alpha and two beta chains only have two stable positions
makes the T to R transition binary*
Give this one a try later!
Origin of Hemoglobin's Cooperativity
Integral (includes lipid-linked): actually inside the membrane, needs detergents to
remove.
Peripheral: on the outside of the membrane, can be removed by salt and pH changes.
Give this one a try later!
Two types of membrane proteins
,High ammonia could be because of an enzyme defect or acute liver crisis.
Give this one a try later!
Urea cycle defects
Lactate produced in skeletal muscle moves to the liver, where it is turned back into
glucose.
Steps:
1 Glucose is converted to pyruvate in the muscle via glycolysis with energy loss. The
pyruvate is then converted to lactate, which is then transferred to the liver, where it is
converted to pyruvate and then glucose via gluconeogenesis and energy input. The
glucose then goes back to the muscle, and the cycle continues!
Give this one a try later!
The Cori Cycle
Hemoglobin has n=2.8, making it extremely cooperative. This gives it a sinusoidal curve
for % saturation vs. PO2. Binding the first O2 is difficult: requires 18 mmHg. However,
the second is easier, it requires 26 mmHg. From there, the last two are much easier.
Myoglobin, on the other hand, is not cooperative. This gives it a hyperbolic curve for
% saturation vs. PO2.
Give this one a try later!
, Hemoglobin vs. Myoglobin: cooperativity
Fibrous proteins have a single major type of secondary structure, while most other
proteins are folded compactly and have a mix of secondary structures.
Give this one a try later!
Fibrous vs. globular proteins
The Mitchell Hypothesis: the energy released when protons come back into the
matrix via ATP synthase drives the synthesis of ATP. Protons are pumped out of the
membrane in complexes 1 (4 H+) 3 (4 H+) and 4 (2 H+) of the ETC, and they flow back
across the membrane with their electrical gradient (negative interior) and their
concentration gradient (alkaline interior). When they enact this "proton motive force"
and come back into the membrane via ATP synthase channel, the energy created
drives ATP synthesis.
Give this one a try later!
Chemiosmotic Theory
Integral building blocks of the extracellular matrix, or ECM, which is the complex
meshwork outside cells that provides cellular scaffolding and is crucial in tissue
development and homeostasis. They serve as cartilage shock absorbers, eyeball
lubricant, and a method by which skin can retain moisture.
They are heteropolymers of amino sugars and negatively charged sugars (sulfate
groups and/or carboxylate groups). They have lots of negative charges, so the chain
forms an extended rod-like helix that attracts Na+ ions and H2O.
2 NADH, 2 ATP, 2 NADH
TCA
6 NADH, 2 FADH2, 2 ATP
ETC/OXPHOS:
Lots of ATP
Give this one a try later!
, Cellular Respiration: Energy output per glucose
Structures of oxygenated (R state) and de-oxygenated (T state) hemoglobin differ.
The T state, or the de-oxygenated form of hemoglobin, is more stable in the absence
of O2 because of several key interactions (including ion pairs) that do not exist in the
R state.
However, when deoxy-hemoglobin binds O2, it undergoes a conformational change
that breaks many of these interactions. O2 pulls iron into the heme plane, which drags
His-F8, and the rest of the molecule, with it, giving the R state, or the oxygenated
form of hemoglobin that has a higher affinity for other O2 molecules. After the initial
bind, the second, third, and fourth O2 molecules bind at lower partial pressure
increments!
*The fact that the two alpha and two beta chains only have two stable positions
makes the T to R transition binary*
Give this one a try later!
Origin of Hemoglobin's Cooperativity
Integral (includes lipid-linked): actually inside the membrane, needs detergents to
remove.
Peripheral: on the outside of the membrane, can be removed by salt and pH changes.
Give this one a try later!
Two types of membrane proteins
,High ammonia could be because of an enzyme defect or acute liver crisis.
Give this one a try later!
Urea cycle defects
Lactate produced in skeletal muscle moves to the liver, where it is turned back into
glucose.
Steps:
1 Glucose is converted to pyruvate in the muscle via glycolysis with energy loss. The
pyruvate is then converted to lactate, which is then transferred to the liver, where it is
converted to pyruvate and then glucose via gluconeogenesis and energy input. The
glucose then goes back to the muscle, and the cycle continues!
Give this one a try later!
The Cori Cycle
Hemoglobin has n=2.8, making it extremely cooperative. This gives it a sinusoidal curve
for % saturation vs. PO2. Binding the first O2 is difficult: requires 18 mmHg. However,
the second is easier, it requires 26 mmHg. From there, the last two are much easier.
Myoglobin, on the other hand, is not cooperative. This gives it a hyperbolic curve for
% saturation vs. PO2.
Give this one a try later!
, Hemoglobin vs. Myoglobin: cooperativity
Fibrous proteins have a single major type of secondary structure, while most other
proteins are folded compactly and have a mix of secondary structures.
Give this one a try later!
Fibrous vs. globular proteins
The Mitchell Hypothesis: the energy released when protons come back into the
matrix via ATP synthase drives the synthesis of ATP. Protons are pumped out of the
membrane in complexes 1 (4 H+) 3 (4 H+) and 4 (2 H+) of the ETC, and they flow back
across the membrane with their electrical gradient (negative interior) and their
concentration gradient (alkaline interior). When they enact this "proton motive force"
and come back into the membrane via ATP synthase channel, the energy created
drives ATP synthesis.
Give this one a try later!
Chemiosmotic Theory
Integral building blocks of the extracellular matrix, or ECM, which is the complex
meshwork outside cells that provides cellular scaffolding and is crucial in tissue
development and homeostasis. They serve as cartilage shock absorbers, eyeball
lubricant, and a method by which skin can retain moisture.
They are heteropolymers of amino sugars and negatively charged sugars (sulfate
groups and/or carboxylate groups). They have lots of negative charges, so the chain
forms an extended rod-like helix that attracts Na+ ions and H2O.
