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72 Cards in this Set

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Ehler-Danlos Type IV
Mostly effects Type 3 collagen fibers. Hence, results in ruptured arteries and ruptured bowel.
Ehler-Danlos Type VI
Cause....
Results in....
Due to deficiency of Lysylhydroxylase.
Results in joint hypermibility and ocular rupture.
Ehler-Danlos Type VII
Cause....
Results in....
Collagen molecules still contain N-terminal ends.
Results in loose packing and improper cross linking. Causes hyperextensible joints and stretchy skin.
Osteogenesis Imperfecta
Causes...
Many causes. One..Replacing Gly with a more bulky group (GLY is small and allows for tight packing)

Mutations near C-terminal are most severe because this is where the triple helix starts winding here.
Menke Syndrome
Cause...
Results in...
Cu+2 deficiency. (because Cu+2 is required for lysyloxidase reactions)
Results in....weak collagen and fragile bones.
Ehler-Danlos Type IV
Mostly effects Type 3 collagen fibers. Hence, results in ruptured arteries and ruptured bowel.
Ehler-Danlos Type VI
Cause....
Results in....
Due to deficiency of Lysylhydroxylase.
Results in joint hypermibility and ocular rupture.
Ehler-Danlos Type VII
Cause....
Results in....
Collagen molecules still contain N-terminal ends.
Results in loose packing and improper cross linking. Causes hyperextensible joints and stretchy skin.
Osteogenesis Imperfecta
Causes...
Many causes. One..Replacing Gly with a more bulky group (GLY is small and allows for tight packing)

Mutations near C-terminal are most severe because this is where the triple helix starts winding here.
Menke Syndrome
Cause...
Results in...
Cu+2 deficiency. (because Cu+2 is required for lysyloxidase reactions)
Results in....weak collagen and fragile bones.
Desmosine
Associated with Elastin fibers.
Residue for 4-lysing groups between two peptide chains.
Heparin
Type of proteoglycan
Found in mast cells.
Activates Anti-thrombin III, thus prevents clot formation.
Haptoglobin
Binds one Hb molecule
Hemopexin
Binds one Heme molecule
Integrin
Cell to ECM.
Laminin and Fibronectin are associated proteins.
Desmosine
Associated with Elastin fibers.
Residue for 4-lysing groups between two peptide chains.
Heparin
Type of proteoglycan
Found in mast cells.
Activates Anti-thrombin III, thus prevents clot formation.
Haptoglobin
Binds one Hb molecule
Hemopexin
Binds one Heme molecule
Protein found in Beta region.
Integrin
Binds cell to ECM.
Laminin and Fibronectin are associated proteins.

Mg dependent. ONLY ONE
Hb McKees Rocks
B chain is 2 amino acid short.
Hb Constant Spring
Alpha chain is 31 amino acids long
Hb Severne
B chain is 10 amino acids long
Marfan Syndrome
Fibrillin defect
Nucleolus
Ribosome subunits are assembled here. Then they are transferred out for translation
Proteome
The complement of proteins expressed by a genome
Definition - Proteomics
STudy of the proteins expressed by a cell, organ or organism.
Where does Trypsin cleave?
On the coboxyl side of Arginine or Lysine AA.
Which two AAs can be created with only one codon?
Methionine and Trp
Endosome functions
1. Endocytosis
2. Storage pool for specific transporters (such as Glucose transporters when Insulin attaches to the receptor).
Describe Alpha helix structure of an amino acid?
H-bond between alpha-amino and alpha-carboxyl group.
3.6 residues per turn.
Side chains pointing to right and left.
Prolines cause bends in polypeptide chains and so disrupt alpha helix.
Give two examples of quarternary structure.
1. Hb
2. Tubulin (alpha and beta tubulins)
Describe "Biological Denaturation" vs "Physical Denaturation"
Biological Denaturation - Minor conformational changes resulting in loss of biological activity.

Physical denaturation - Loss of all secondary, tertiary and quaternary structures.
Chaperonins
Heat-Shock protein.
Protect newly synthesized protein from proteolysis and facilitate correct folding.
Describe the use of "Protein Solubility" principle to separate proteins.
Hydrophobic molecules will clump together (and become insoluble) when water is not available.

Water can be made unavailable by salt (salting out) or ethanol like substance.
Centrifugation is used to separete...
soluble proteins from insoluble cellular components. (spin material at high speed).

(Density gradient centrifugation can be used to separate molecures based on their desities).
Gel Filteration is used to separate...
Larger proteins from smaller proteins. (Smaller proteins get in the gel pores and take longer to hydrate). So larger proteins elute first.
Ion Exchange is used to separte....

Describe two types of ion exchange apparetus
proteins based on their charge.

Cation exchangers - Negatively changed beads
Anion Exchange - Postively charged beads.
Affinity chromatography is used to separate proteins based on their...
Biological functions.(ex - good for Immunoglobulins due to their high affinity to specific antibodies)
X-ray diffraction is used to...
Obtain 3-D structure of a protein. (This technique requires crystallization of the proteins).
Name the polypeptide chains for following Hb types...

HbA1
HbA2
HbF
HbE
HbA1 - alpha2, beta2
HbA2 - alpha2, delta2
HbF - alpha2, gamma2
HbE - zeta2, epsilon2
What is Inosine?
Inosine can penetrate RBC and be converted into BPG. (BPG is depleted in blood due to biological processes).
Methemoglobinemia
Descibe it...
Two causes...
Converts Fe+2 to Fe+3. This Hb Beta chains can not bind to O2.
Two causes...
(1) Proximal His replaced by Tyrosine. So Fe+2 can't bind.
(2) Deficiency of cytochrome b5 reductase enzyme (which reduces Fe+3 to Fe+2).
Menke's syndrome
Caused due to...
Results in...
Cause - Cu+2 deficiency.
Results in fragile bones and weak collagen.
Sarcomere
Defined as area between two z lines.

It gets smaller during contraction. Split in half by M line in the H band.
I Band
Is the region between thick filaments. Split in half by Z line. (it is the light band).
A band
Cotains thick filaments in a sarcomere.
H band
Is the region between two sets of thin filaments. When cell is contracted, the H band disappears.
M Line
Darkest area in the middle (darkest because of the fine thread of filament that holds two myosins together).
Calmodulin
Binds to Ca+2 for smooth muscle contraction. (Note: For skeletal muscle, Ca+2 binds to TnC.)
What is the function of cGMP?
cGMP dependent phosphorylation of MLCK prevents its binding to Ca+2 and contraction. (Hence, it relaxes smooth muscle and so used in viagra).
Titin
Nebulin
Titin - Acts like a spring to keep myosin filaments in center.

Nebulin - Extends the length of F-Actin and regulates its length.
What is polyclonal antisera?
When multiple lymphocytes produce antibodies against different epitopes.
Which chains (on Igs) have carbohydrate chains attached to them? Where?
Heavy chains.

On the Aspargine residue.
What is Papain split?
Papain splot cleaves IgG above disulfide bonds (at the hinge region) and splits the Ig in 2 Fab and Fc regions.
Which is the only Ig that crosses placenta?
IgG
IgA is associated with....

It is found in....

Its structure...
IgA is associated with secretions, saliva, tears and sewat and provides initial defense.

Found in colostrum - breast milk.

Dimer. Linked by a J chain. Has an associated secretory component.
IgE is found on...

IgD is found on...
Mast cells. Causes Mast cells to release histamine.

Surface of B-cells, where it acts as an antigen receptor in signaling B-cells to proliferate.
Radial Immunodiffusion Assays is used to...
Measure the concentration of antigens via precipitation reactions after diffusion in agarose.
Immunoelectrophorosis is used to...
Detect gross changes in the levels of plasma proteins to diagnose diseases such as multiple myeloma.
Enzyme linked immunoabsorbent assays is used to...
Provide quantitative data on the concentrations of proteins and other antigens.
What is "Waldenstrom's Macroglobulinemia"
Patient's blood becomes very viscus because this disease is a multiple myeloma involving a cancerous plasma cell that produces excessive amount of IgM.
What are Major histocompatibility complexes?
Important for immune system to recognize our own proteins (versus foreign objects)

Matching Class I MHCs is vital for successful organ transplant.
Ornithine
AA created by post-transitlational modification.

(Add H2O to Arginine) - Ornithine is one CH2 group less than Lysine.
Which AA change results in sickle cell anemia?
Glu to Val (hydrophilic to hydrophobic)
Salt bridges are between...
Carboxyl groups and Amino groups.
Hydrophobic bonds are between...
Aromatic rings and carbon side chains (Tryptophan and Leucine being an example)
How will following reagents denature proteins?

8M Urea
6M Guanidine HCL
B-Mercapoethanol
Acetone
Heat
SDS
8M Urea - Break H-bonds
6M Guanidine HCL - Break H bonds
B-Mercapoethanol - Break disulfide bonds
Acetone - Disrupt hydrophobic interactions
Heat - Break H-bonds
SDS - Complete denaturation of the protein.
What is the charge on the SDS treated proteins?
Negative (constant charge to mass ratio) - Hence, this treatment is used for electrohorosis.
BPG

Charge...
Binds to...
Stabilizes this form of Hb
Negative charge.
Binds to (HIS, LYS) on beta chains.
Stabilizes the tight form of Hb.
Decreases O2 affinity, so good for O2 delivery.
Alpha 1 region proteins
A1 - Antritrypsin (inhibit elastase)
A1 - Antichymotrypsin (inhibit PMN cathespin G)
A1 - acid glycoprotein
Alpha keratin is in....
Beta keratin is in...
Hair and wool
Skin and nail