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58 Cards in this Set

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What level of protein structure has maximally extended structures with phi and psi angles defined as zero?
What type of protein structure has intra chain H-bonding?
What are the three types of secondary protein structures?
Helical (alpha-helix)
Beta (maximally extended primary sequence)
Random Chain( interactions between R groups)
Helical and Beta secondary structures are due to the H-bonding between atoms in what bond?
peptide bond
How are Beta-barrels formed?
When Beta-sheets roll on themselves (super secondary structure)
What is a super secondary structure?
The result of localized folding of secondary structures that are due to interactions of multiple secondary domains.
What are two common super secondary structures?
Helix loop Helix (transcription factors)
and Beta-barrel
What is the difference between super secondary structures and tertiary structures?
Super secondary structures have localized folding domains that may have structural or functional significance in that area. Tertiary structures occur when the whole protein is affected by folding.
What are the two types of Tertiary Protein structures?
Globular and Fibrous
What are the differences between Globular and Fibrous tertiary protein structures?
Globular: functional (enzymes)
variety of different kinds of secondary structures

Fibrous: structural
one dominating kind of secondary structure
What forces are involved in maintaining a Tertiary structure?
1.Hydrogen bonds
2. van der Waals forces(repulsion forces of like chargers, weakest alone but can build up)
3. Hydrophobic interactions (repelled by water, pushed into interior of structure)
4.electrostatic forces (salt bridges formed by charged groups on the structure)
What protein structure is only found in multisubunit proteins?
Quaternary structure
What is a quaternary protein structure?
The overall orientation of the polypeptides as a consequence of those polypeptides interacting with one another.
Primary function of myoglobin?
To store oxygen in muscles for release in periods of oxygen deprivation (short rapid bursts, muscle twitching)
Primary function of hemoglobin?
Carry oxygen from lungs to tissue and to bring CO2 from tissue to lungs.
What is the difference in subunits between hemoglobin and myoglobin?
Hemoglobin has 4 subunits so it can carry 4 moles of oxygen.
Myoglobin has one subunit so it can only carry 1 mole of oxygen.
What are the hemoglobin subunits composed of?
2 alpha and 2 beta subunits, all 4 have an iron complex to heme.
Oxygen binds to what to form Heme B?
Oxygen binds to the iron portion of protoporphyrin IX.
What are the four primary regulators of oxygen binding to hemoglobin and what kind are they all? Why are they important?
Negative regulators.
1. CO2
2. 2,3-BPG
3. H+
4. Cl-
Important in releasing oxygen to the surrounding tissues
Poor binding of oxygen to hemoglobin is know as what kind of state?
T-state or tense state which means hemoglobin has a reduced affinity for oxygen
Oxyhemoglobin tetramers are in a high binding state known as?
R-state (relaxed state) where they have an increased affinity for oxygen
What affect does CO2, 2,3-BPG, H+, and CL- have on hemoglobin?
They increase the proportion of T state
How is the R-state effected as oxygen is binded to each subunit of hemoglobin?
R state of the overall hemoglobin will increase as each subunit binds oxygen.
HbF stands for what?
Fetal hemoglobin
Why does fetal hemoglobin have a higher affinity for oxygen than adult hemoglobin?
It has to compete for oxygen with adult hemoglobin in maternal blood so has to have higher affinity since it is the only way for the fetus to receive oxygen.
How is CO2 bound to hemoglobin when transported from the tissues to the lungs?
Transported by a covalent attachemnt to amide nitrogens forming carbamino-Hb.
What happens to the CO2 on hemoglobin once it reaches the lungs?
The high partial pressure of O2 favors the R-state which leads to the release of the CO2.
What is the Bohr effect?
Increases in hydrogen ion concentration decrease the amount of oxygen bound to hemoglobin at any oxygen concentration.
Tissues have a decreased pH due to?
formation of bicarbonate by RBCs
A decrease in pH levels in tissues will lead to?
1.an increase in H+ which leads to
2. nitrogen groups on the hemoglobin becoming charged
3. which changes the conformation from more R to more T
4. which pushes the oxygen off and into the tissues.
In the Bohr effect what can the H+ ions interact with and ionize?
N-terminal amino acid groups of alpha chains and imidazole groups(nitrogen) of Histanine in alpha and beta chains
What is the chloride shift?
When bicarbonate is released from the RBC a huge charge differential is made since it has a (-) charge. Cl- counters this movement by entering the RBC thus a shift of negative charges is made.
What is a hemoglobinopathy?
What happens if hemoglobin doesn't work properly.
What kind of hemoglobin genes are there?
alpha and beta globin gene clusters
What is the direction of the globin gene cluster developmental pattern of expression?
5' -> 3'
What is the major site of hemoglobin in a fetus and as an adult?
In the fetus it is the liver and spleen and after birth the bone marrow takes over.
HbA2 is a measure of what?
fetal hemoglobin found in adult blood.
What can be helpful in separating different types of hemoglobin genes in blood?
hemoglobin electrophoresis
What does HbA1c measure and what is it useful in diagnosing?
Measures how much glucose is in the blood and is useful in diagnosing diabetes type II
What types of mutations are there in Hemoglobin genes?
Qualitative and Quantitative
What is an example of a qualitative abnormality in a globin gene?
Sickle cell anemia
What is another name for a quantitative abnormality of a globin gene and what are the 2 classes?
alpha-thalassemia (loss or reduction of alpha-hemoglobin gene)
beta-thalassemia (loss or reduction of beta-hemoglobin gene)
Both Hemoglobin S and Hemoglobin C mutations occur at which codon?
Codon 6 on the adult beta-globin gene.
What causes genes to stick together and form the sickle shape in Hemoglobin S mutations?
The glutamic acid is changed to a valine which changes a hydrophilic gene to a hydrophobic gene. The valines interact with one another and stick together.
What causes the sickle cells to lysis?
The sickle shape causes the membrane to weaken and distort which will cause the RBCs to lysis which causes the hemolytic anemia part of sickle cell anemia.
What happens in the Hemoglobin C mutation?
Glutamic acid is changed to lysine (+ to - charge) but both are hydrophilic so no major change in cell shape. Relatively benign mutation.
What type of disorder is sickle cell anemia?
autosomal recessive disorder
What is special about sickle cell anemia in regards to genotype and phenotype?
It has a recessive genotype, but a dominant phenotype. Meaning that a heterozygous individual can still manifest sickle cell disorder.
What are symptoms of sickle cell anemia (6 items)?
1.hemolytic anemia (low hematocrit)
2. hyperbilirubinemia resulting in jaundice and icterus (brain damage due to build up of bilirubin in brain)
3. reticulocytosis (increased immature RBCs)
4. vaso-occlusive crisis due to hypoxic injury in tissues
5. increased susceptibility to infection (bone marrow isn't functioning properly, leukopenia)
6. chronic hypoxia leads to impaired growth and development and organ damage
The genes for various hemaglobinopathies have survived because it gives a somewhat immunity to what other disease and why?
malaria, since it travels and survives on the RBC. In individuals with various hemaglobinopathies the RBC is often weak and damaged so this gives malaria less of a chance to thrive and allows the host to time survive and reproduce and pass on their genes.
Thalassemias are what type of hemoglobinopathy?
What is HbH disease?
An alpha-thalassemia/ an absence of 3 of 4 alpha subunits which leads to beta-tetramers.
What is Hb Bart'?
an alpha-thalassemia in which no alpha subunits are present and leads to hydrops fetalis and neonatal death
An absence of both beta-subunits of hemoglobin leads to what?
It is a beta-thalassemia and leads to alpha tetramers which are very unstable and RBCs destroyed in sleep and bone marrow.
HbA1c is what?
glycosylated hemoglobin
How long is the life-cycle of a RBC?
120 days
What is your HbA1c levels used in diagnosing?
Type 2 diabetes
What is the normal percentage for HbA1c?
less than 7%