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81 Cards in this Set
- Front
- Back
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What is Mb composed of?
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A heme group + globin protein
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How many turns does Mb have?
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8 turns
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How many AAs does Mb consist of?
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153
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His F8 means?
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Histidine is the 8th AA residue in the F coil.
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What is the importance of the NO?
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it is a vasodilator, and it also inhibits platelet aggregation.
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Hemoglobin consists of .... polypeptide chain
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4, Tetrameric
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How many helical segments do the alpha & beta chains of Hb have?
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1- 7 segments in alpha helices.
2- 8 segments in beta-helices. |
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Adult hemoglobins are:
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Hb A1
Hb A2 |
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What does the HB A1 consist of?
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2 alpha chains
2 beta chains |
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What does Hb A2 consist of?
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2 Alpha chains
2 Delta chains |
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What does Hb F consist of?
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2 Alpha chains
2 Gamma chains |
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Embryonic Hb is made of?
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2 alpha chains
2 epsilon chains |
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How many heme prothetic groups can we find in Hb and Mb?
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Hb --> 4
Mb --> 1 |
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allosteric inhibitors of Hb are:
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1- Decrease in the PH.
2- Increase in co2 concentration. 3- an increase in 2,3 bisphosphoglycerate concentration. |
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An example of the allosteric activators of HB is
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CO
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What do we add to replenish 2,3 BPG in stored blood?
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Inosine
dihydroxyacetone phosphate |
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What is the location of Hb & Mb?
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Hb: RBCs
Mb: Muscles |
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What si the function of each of HB & Mb?
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Hb: O2 carrier.
Mb: O2 reservoir |
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What is the structural difference between Hb & Mb?
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Hb: Tetramer(Quaternary structure)
Mb: Monomer(No Quaternary) |
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Can Mb carry any molecules other than O2?
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No, but Hb can.
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Which protein shows oxygen cooperativity?
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Hb
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Which proteins has a higher O2 affinity?
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Mb
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Dissociation curve of Hb is
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Sigmoid
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Dissociation curve of Mb is
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Hyperbolic
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Is Mb affected by allosteric effectors?
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No
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Abnormalities in the primary sequence of AAs in the globin chains leads to
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Hemoglobinopathies
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Abnormalities in the rate of synthesis of globin results in
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Thalassemia
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Sickle cell Anemia is a result of
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Substitution of Glutamate with Valine in the beta chains, position # 6
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Hb S is
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Sickle cell anemia
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The Average lifespan of RBCs HbS
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10-15 Days
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Which AAs are substituted in Hb C?
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#6 glutamate is substituted by Lysine residues, results in mild chronic hemolytic anemia.
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What are the types of thalassemia?
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Alpha thalassemia
Beta Thalassemia |
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Collagen represents about ..... of body proteins
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third
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What are the carbohydrate residues that collagen contains?
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glucose
galactose |
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What are the AAs in which collagen is rich?
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Glycine(35%)
Proline Hydroxyproline Hydroxylysine(21%) Alanine(11%) |
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What does the hydroxylation of proline and lysine require?
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Ferrous Iron
Molecular Oxygen Ascorbate |
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What is the AA sequence in collagen?
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Gly-X-Pro
Gly-X-HyPro |
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The basic structural unit of collagen is
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tropocollagen
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The three polypeptide chain of tropocollagen are
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supertwisted around each other
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Where is Type I collagen present?
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Bones, Skin, Tendons, & heart valves
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What's special about type I collagen?
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It contains two identical polypeptides but the third is different
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Where can we find type II collagen?
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Vitreous humor
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Where can we find type III collagen?
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Blood vessels
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Where can we find type IV collagen?
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Basement membrane
Lens capsule |
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Type II, III, IV show
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Identical three polypeptides
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Where can we find type V collagen?
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exocytoskeleton(three different polypeptides)
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Vitamin C deficiency leads to scurvy because
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It is important for the hyroxylation of lysine and proline, which increase the stability of collagen.
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Osteogenesis imperfects is due to:
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single glycine mutation, glycine in very important for the stability of collaen.
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Where can we find Alpha keratin?
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Epidermal layer of skin
Hair Nail |
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What gives keratin fibers their strength?
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The great number of present disulfide bonds, Keratins are rich in cysteine residues.
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Give an example of beta keratins?
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Fibrion, which is a silk protein, is rich in glycine and alanine
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Name some tissues which are rich in elastic fibers
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Aorta
various ligaments the lungs vascular tissues |
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the basic subunit of elastin fibrils is
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tropoelastin
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How does tropoelastin differ from tropocollagen
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It has many lysine and few proline residues.
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The cross-links of elastin involve
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Desmosine
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Desmosine joins tropoelastin chains into
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arrays that can be stretched reversible in all directions
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Salting out depends on
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decreased solubility of different proteins at high salt concentration
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Why is ammonium sulfate used in salting out?
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because it's very soluble and is effective at lower concentrations than any other salt
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1/4 saturated ammonium sulfate solution perciptates
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Fibrinogen
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Half saturated ammonium sulfate solution perciptates
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globulins
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Fully saturated ammonium sulfate solution perciptates
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albumin
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Dialysis membranes are made of
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cellophane or celloidin
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Ultracentrifugation depends on
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protein mass
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Dialysis depends on
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proteins' large size
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Lipoproteins are ultracentrifugated into
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chylomicrons, VLDL, LDL, HDL.
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Ribosomes are separated into
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30 S & 50 S subunits in prokaryotes.
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Electrophoresis separates proteins according to their
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charge
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The bands of proteins are stained by .... after electrophoresis
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ponceau S
coomassie blue |
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At pH of 8.3, plasma proteins will have a .... charge
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negative, they will migrate to the anode
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Isoelectric focusing separates proteins depending on the basis of
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the difference in their isoelectric points
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ampholytes
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amino acids, carboxylic acids
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The pH gradient is established by placing the proteins in an
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aqueous mixture of synthetic low weight ampholytes
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What's the importance of SDS in electrophoresis?
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It denatures the proteins and forms negatively charged micelles with proteins
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SDS electrophoresis depends on
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molecular weights
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resins are
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beads which have pores of differents sizes
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In Ion-exchange chromatography resins carry .... charge and are called
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Negative cation exchangers
Positive anion exchangers |
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In affinity chromatography, ligands are
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covalently boned to resins
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myfibrils consist of
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sarcomere
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Myosin is
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Assymetric hexamer consisting of two heavy chains and four light chains
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A hapten is
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a small molecule that can't alone eelicit an antibody response
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Epitope is
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a small molecular structure within the antigen to which the antibody binds
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