Term
What is the angle between Hydrogens in water? |
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Definition
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Term
What is the molarity of pure water? |
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Definition
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|
Term
What is the equilibrium constant for water? |
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Definition
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Term
What is the key function of a peroxisome? |
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Definition
Lipid metabolism (oxidation/degredation and synthesis)
*Other roles include synthesis of glycerolipids, plasmogens, and isoprenoids) |
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Term
What enzyme catalyzes hydrogen peroxide to oxygen and water, as well as oxidation of various compounds by hydrogen peroxide (such as methyl groups)? |
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Definition
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Term
What are the two most important buffers in the body? |
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Definition
Carbonic acid and Phosphoric acid
H2CO3 and H3PO4 |
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Term
What is the pH of blood plasma? Interstitial fluid? Cytosol? |
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Definition
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Term
What is the pH of lysosomal matrix? Gastric juice? Pancreatic juice? |
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Definition
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Term
What is the pH of human milk? Saliva? Urine? |
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Definition
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Term
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Definition
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Term
What physical property of CO2 makes it easily expelled at varying rates of respiration? |
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Definition
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Term
What is the k3 value for the bicarbonate buffer system? |
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Definition
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Term
What is the pK3 of the bicarbonate buffer system? |
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Definition
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Term
T/F Prokaryotes have an inner and outer membrane? |
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Definition
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Term
Name four features of an amino acid. |
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Definition
1. Asymmetric carbon 2. Carboxyl group 3. Amino group 4. Side chain (which is hydrophobic, hydrophilic, charged, and/or neutral) |
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Term
What is the abbreviation and single letter code for the following amino acids: glycine, alanine, valine, leucine, isoleucine? |
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Definition
glycine - Gly G alanine - Ala A valine - Val V leucine - Leu L isoleucine - Ile I |
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Term
What is the abbreviation and single letter code for the following amino acids: proline, phenylalanine, tyrosine, tryptophan, methionine? |
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Definition
proline - Pro P Phenylalanine - Phe F Tyrosine - Tyr Y Tryptophan - Trp W Methionine - Met M |
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Term
What is the abbreviation and single letter code for the following amino acids: serine, threonine, cysteine, asparagine, glutaminme, aspartate, glutamate, lysine, arginine, and histadine? |
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Definition
serine - Ser S threonine - Thr T Cysteine - Cys C Asparagine - Asn N Glutamine - Gln Q Aspartate - Asp D Glutamate - Glu E Lysine - Lys K Arganine - Arg R Histadine - His H |
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Term
What chemical property of a peptide bond makes it fixed and unable to rotate? |
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Definition
Resonance (between the carbonyl carbon and the oxygen and nitrogen it is attached to) |
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Term
What is the torsion angle in the trans conformation of a peptide? |
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Definition
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Term
What type of bond occurs between cysteine residues of adjacent AA's? |
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Definition
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Term
Which peptide bond conformation is more energetically favorable cis or trans? |
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Definition
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Term
Define the isoelectric point. |
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Definition
The average of the two pK values involved in the formation of the zwitterionic form. |
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Term
If the pH is greater than the isoelectric point than a molecule has what charge? |
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Definition
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Term
Where is the site of the synthesis of proteins and enzyme metabolic pathways? |
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Definition
Cytoplasm (as per lecture slides) |
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Term
What is the most soluble amino acid? |
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Definition
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Term
What are the two most prevalent anions in the extracellular fluid? |
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Definition
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Term
T/F Most proteins have a negative charge at a pH of 7.4. |
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Definition
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Term
Through what does the outer surface of a cell make adhesive interactions with the extracellular matrix? |
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Definition
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Term
What are the enzymes present in the smooth ER that are involved in lipid synthesis? |
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Definition
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Term
What organelle is responsible for the production of glycoproteins? |
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Definition
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Term
What permits larger molecules into the outer membrane of the mitochondria? |
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Definition
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Term
What are the main group of enzymes found in lysosomes? |
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Definition
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Term
What occurs during "I cell disease"? |
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Definition
Cellular mechanisms for storing lysosomal enzymes in lysosomes is disrupted and instead diffuses into the ECM damaging everything around it. |
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Term
What two types of mammalian insulin most closely resembles human insulin? |
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Definition
Dog and Porcine (pig), which both have only a 1 amino acid difference. |
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Term
T/F Quaternary structures do not have ANY covalent bonds. |
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Definition
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Term
How many amino acids per 360 degree turn do alpha helices have? |
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Definition
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Term
What are the two types of beta pleated sheets? |
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Definition
Parallel and anti-parallel |
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Term
In which beta sheet conformation are the hydrogen bonds planar? |
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Definition
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Term
What was the first mitochondrial disease discovered? |
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Definition
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Term
What kind of disease is Leber's Hereditary Optic Neuropathy? |
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Definition
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Term
What is an abnormality in which uric acid is produced in excess and why do the symptoms occur? |
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Definition
Gout - Symptoms occur because uric acid crystals build up in joints and lysosomal enzymes burst with too much uric acid, causing cell lysis. |
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Term
What is the cause of Cholesteryl Ester Storage Disease (CESD) and Wolfman's Disease? What type of disease is it? |
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Definition
Genetic deficiency of hLAL (human lysosomal acid lipase).
Autosomal recessive |
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Term
What is a rare autosomal recessive disease characterized by decreased levels of plasmalogens, increased levels of long chain fatty acids, and cholestanoic acid derivatives? Give the main type of disorder and the most severe. |
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Definition
Peroxisome Biogenesis Disorders (PBD)
Zellweger's Disease |
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Term
When looking at electrophoretic analysis of plasma proteins, what does a delayed response indicate? |
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Definition
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Term
What is the designation for the variant form of hemoglobin in which a nonconservative substitution occurs in the 6th position of the b-globin chains? |
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Definition
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Term
In sick cell anemia what is the non-conservative substitution that takes place? |
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Definition
Valine replaces Glutamic acid |
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Term
What is the best analytical determination of sickle cell anemia and why? |
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Definition
Gel electrophoresis because the lack of glutamic acid makes HbS less acidic and therefore it does not migrate as quickly to the anode. |
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Term
Ehlers-Danlos syndrome, osteogenesis imperfecta, and scurvy are all examples of what type of disease? |
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Definition
Diseases of Collagen Synthesis |
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Term
What is the cause of type 1 hyperlipidemia? |
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Definition
Accumulation of chylomycrons. |
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|
Term
What is the cause of type 2 hyperlipidemia? |
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Definition
Elevated levels of LDL caused by genetic defects in the synthesis, processing, or function of the LDL receptor. |
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Term
What is the cause of type 3 hyperlipidemia? |
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Definition
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|
Term
What is the cause of type 4 hyperlipidemia? |
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Definition
Increased VLDL levels due to obesity, alcohol abuse, or diabetes. |
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Term
What is the most common form of hyperlipidemia? |
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Definition
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Term
What is a genetic disease that is characterized by absence of chylomicrons, VLDL, and LDL due to an inability to synthesize apolipoproteins apoB-100 and apoB-48? |
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Definition
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|
Term
What rare autosomal recessive disease causes a deficiency of a-lipoprotein? |
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Definition
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Term
The changes in concentration of what in diabetes patients can be used to follow the effectiveness of treatment for the diabetes? |
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Definition
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Term
What are proteins that act as infectionus agents in the absence of DNA or RNA? |
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Definition
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Term
What is the most common prion disease? |
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Definition
Creutzfeldt-Jakob disease |
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Term
What prion protein is conformationally changed in Creutzfeldt-Jakob disease? |
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Definition
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|
Term
What is a typical molarity of [HCO3-]? |
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Definition
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Term
What diseases are caused by enlarged lysosomes, full of undigested material? |
|
Definition
Lysosomal storage diseases |
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Term
In HbS what occurs in the deoxy form that cases problems? |
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Definition
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|
Term
The formation of covalent cross links in collagen requires what? |
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Definition
Conversion of some e-amino groups of lysine to aldehydes. |
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Term
Abetalipoproteinemia is a disease in which chylomicrons, VLDL, and LDL are absent from the blood because of an inability to synthesize what? |
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Definition
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Term
What class of immunoglobins is found mainly in mucosal secretions? |
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Definition
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Term
What immunoglobin class is the initial defense against invading viral and bacterial pathogens prior to their entry into plasma or other internal space? |
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Definition
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Term
What is the first antibodies produced in significant quantity on exposure to a foreign antigen? |
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Definition
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Term
What two immunoglobin classes promotes phagocytosis of microorganisms? |
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Definition
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Term
What immunoglobin plays an important role in allergic responses? |
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Definition
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Term
What are inactive precursor serine proteases? |
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Definition
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Term
What serine protease acts directly on fibrin to degrade a clot? |
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Definition
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Term
Administration of what shortly after an MI significantly enhances recover? |
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Definition
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Term
Which serine protease is believed to be required for metastasis of cancer cells? |
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Definition
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Term
T/F Mitochondria are associated with apoptosis? |
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Definition
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Term
T/F Peroxisomes have a role in oxidation of D-amino acids. |
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Definition
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Term
T/F Peroxisomes have a role in hydrolysis of cholesteryl ethers. |
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Definition
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Term
What is the term for two sequences that are highly alignable? |
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Definition
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|
Term
What is a substitution of one AA for another that is of similar polarity? |
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Definition
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Term
What is a substitution of one AA for another that is of dissimilar polarity or geometric configuration? |
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Definition
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|
Term
How is human insulin made available? |
|
Definition
genetically engineered bacteria |
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Term
What is the only protein structures (group) that does not have covalent bonds? |
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Definition
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Term
Around what bonds is there rotation in peptides? |
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Definition
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Term
What bond is between the alpha carbon and the carbonyl carbon? What about the alpha carbon and nitrogen? |
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Definition
alpha carbon to carbonyl carbon --> psi
alpha carbon to nitrogen --> phi |
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Term
What is the Hill coefficient and what is the formula? |
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Definition
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|
Term
Peptide bond planes are ______ to the alpha-helix axis. |
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Definition
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Term
In an alpha helix how many hydrogen bonds form between AA's and where do they occur in the helix? |
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Definition
Two hydrogen bonds, one to the 4th AA above and one to the 4th AA below. |
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Term
In an alpha helix side chains are found _______ of the spiral structure. |
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Definition
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Term
Explain the protein classification: class. |
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Definition
Based on predominant type of secondary structure. (a-helices, b-sheets) |
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Term
What protein domain classification deals with arrangements of secondary structures within the domain? |
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Definition
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|
Term
What protein domain classification deals with the sequence identity between proteins? |
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Definition
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Term
What type of proteins have spheroidal shapes, high water solubility, and act as transporters and catalysts? |
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Definition
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Term
What kind of proteins contain larger amount of secondary structure, long cylindrical shapes, and low water solubility? |
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Definition
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Term
What are the 2 largest constituents of collagen? |
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Definition
Glycine (33%) and proline (13%) |
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Term
What sequences are repeated several hundred times in collagen? |
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Definition
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|
Term
What is covalently attached to the hydroxyl group of hydroxylysine in collagen? |
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Definition
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|
Term
What is responsible for the highly twisted extended helix of collagen? |
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Definition
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Term
The plane of peptide bond, in collagen, is _____ to the helix correctly oriented to form strong _____ bonds with other polyproline helical polypeptides. |
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Definition
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|
Term
How many polypeptide chains are wound in a superhelical structure in collagen? |
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Definition
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|
Term
How are polypeptide chains in collagen held together? |
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Definition
Hydrophobic interaction with glycines on apolar edge and lysine linkages |
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Term
What are the two non-covalent forces leading to protein folding? |
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Definition
hydrophobic interaction and hydrogen bonding |
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Term
Collagen makes up what percentages of skin, cornea, liver, heart, cartilage, and lungs? |
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Definition
Skin - 74% Cornea - 64% Cartilage - 50% Heart - 12-24% Lungs - 10% Liver - 4% |
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Term
What provides organs and tissues with elastic support in terms of stretching without tearing? |
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Definition
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Term
T/F Elastin does not contain Gly-Pro-Y or Gly-X-Hyp as does collagen. |
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Definition
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Term
Elastin lacks _____ structure but contains unordered coiled structure. |
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Definition
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Term
Elastin contains what kind of crosslinks between which residues? |
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Definition
Contains covalent crosslinks between Lysine residues. |
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Term
What is responsible for blood type? |
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Definition
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|
Term
What are the three main types of covalent linkages of carbohydrates to proteins? |
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Definition
N-glycosyl linkage to asparagine O-glycosyl linkage to serine O-glycosyl linkage to 5-hydroxylysine |
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Term
What is the main type of glycosyl linkage seen in mammals? |
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Definition
Type 3 - O-glycosyl linkage to 5-hydroxylysine |
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Term
What is the most used protein analysis? |
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Definition
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|
Term
What analytical technique separates proteins based on charge? |
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Definition
ion exchange chromatography and polyacrylamide gel electrophoresis (non-denatured technique) |
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Term
What analytical technique separates proteins based on molecular weight? |
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Definition
Gel permeation chromatography and polyacrylamide gel electrophoresis (denatured form) |
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Term
What analytical technique separates proteins based on binding affinity? |
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Definition
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|
Term
In polyacrylamide gel electrophoresis you can separate proteins in two forms. What two forms and how are they separated in each? |
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Definition
Denatured - Based on MW Non-denatured - based on charge |
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|
Term
What separates proteins on the basis of charge to mass? |
|
Definition
capillary electrophoresis |
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|
Term
What is the condition where there is elevated levels of AA's in the blood? |
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Definition
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|
Term
What is the name of the disease that is characterized by a deficiency of tryptophan? |
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Definition
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|
Term
Name three types of proteases used in protein analysis. |
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Definition
Trypsin, chymotrypsin, and cyanogen bromide |
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|
Term
What is the science of protein synthesis and analysis? |
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Definition
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|
Term
What type of analytical technique can separate all of the proteins in a cell? |
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Definition
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|
Term
What two ways does 2D electrophoresis separate proteins? |
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Definition
1st dimension - isoelectric focusing 2nd dimension - mass |
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|
Term
What is the first step in Edman degredation? |
|
Definition
Cleaving of the first amino acid at the N-terminus. |
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|
Term
What are three denaturing agents? |
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Definition
urea, sodium dodecyl sulfate, and guanidine HCl |
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|
Term
What is the most common disease of human transmissible spongiform encephalopathies? How many forms are there? What is the most common pathway to the disease? |
|
Definition
Creutzfeldt-Jakob disease 4 Sporadic (85%) |
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|
Term
What causes human transimissible spongiform encephalopathies? (what prion protein) |
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Definition
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|
Term
What is a coil of several fibrils called? |
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Definition
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|
Term
Amyloid fibrils are made of helical ______ of strands ________ to a cylindrical axis. |
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Definition
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|
Term
What is the only AA capable of a disulfide bond? |
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Definition
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|
Term
Disulfide bonds fall into what categorical structure of proteins? |
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Definition
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|
Term
What are immunoglobins produced by? |
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Definition
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|
Term
How many peptides are typically in light and heavy chains? |
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Definition
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|
Term
How are immunoglobin's polypeptide chains held together and how many are there? |
|
Definition
Disulfide bonds
2 holding the constant regions together and 1 on each of the light chains linking it to the heavy chain (total of 4) |
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|
Term
What is a small molecule to which an antibody can bind but can only elicit an antibody production if bound to a larger molecule? |
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Definition
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|
Term
Haptens bind to macromolcules through what type of bonds? |
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Definition
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|
Term
What is the minimal number of amino acids in sequence that allows binding to antibodies? |
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Definition
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|
Term
What is a typical antibody production? |
|
Definition
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|
Term
The constant domains of immunoglobins are divided into what 3 groups? |
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Definition
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|
Term
How does an immunoglobin go about crossing the placental membrane? |
|
Definition
Constant regions bind complement |
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|
Term
Heavy and light polypeptide chains have _____ AA repeats that are not completely ______. |
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Definition
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|
Term
How many repeats in the light and heavy chains of immunoglobins are there? |
|
Definition
2 in light chains and 4 in heavy |
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|
Term
Each fold of an immunoglobins structure contains ___ beta pleated sheets that are aligned ______. |
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Definition
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|
Term
What is the most common immunoglobin? |
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Definition
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|
Term
Which immunoglobin is present in the highest concentration (mg/mL)? |
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Definition
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|
Term
What is the name of the chain that is linked by two disulfide bonds and links immunoglobins together? |
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Definition
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|
Term
What analytical technique is used to identify immunoglobins? |
|
Definition
ELISA
enzyme linked immunoglobin substrate assay |
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|
Term
What type of binding associates antigens to the antigens binding site? |
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Definition
hydrophobic interactions, van der waals, and hydrogen bonds |
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|
Term
What is a class of enzyme that cleaves peptide bonds? |
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Definition
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|
Term
What do serine proteases contain in the active site? |
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Definition
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|
Term
What are the two different pathways to coagulation? |
|
Definition
Intrinsic - contact factors 7 and 9 Extrinsic- tissue formation
Both use contact factor 10 |
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|
Term
What are the 2 zymogens and 2 active proteins used in clot formation (not the factors, just the main proteins) |
|
Definition
Prothrombin --> Thrombin
Fibrinogen --> Fibrin
Thrombin catalyses the formation of fibrinogen to fibrin |
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|
Term
What is the protein responsible for dissolving a clot? |
|
Definition
Plasmin (the zymogen form is plasminogen) |
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|
Term
|
Definition
t-PA (tissue plasminogen activator) |
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|
Term
What are the two AA's present in a serine protease responsible for cleavage? |
|
Definition
Histadine and aspartic acid |
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|
Term
What is an aspartic protease composed of two identical monomers? |
|
Definition
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|
Term
Hemoglobin is composed of how many and which polypeptide chains? |
|
Definition
alpha and beta
2 alpha and 2 beta make up a hemoglobin |
|
|
Term
What is the 5th bond to in the iron of hemoglobin? |
|
Definition
|
|
Term
How is the heme bound to each protein subunit? |
|
Definition
via 18 apolar AA's via hydrophobic association |
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|
Term
How many alpha helices make up the alpha and beta subunits of hemoglobin? |
|
Definition
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|
Term
What is the effect called when as the pH of the blood drops O2 becomes less willing to bind to hemoglobin? |
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Definition
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|
Term
What happens to the structure of hemoglobin as more O2 binds and what is this called?? |
|
Definition
Tertiary and Quaternary structures change
cooperative binding |
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|
Term
By what angle does the oxy form change in relation to the deoxy form? |
|
Definition
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|
Term
What is the designation for hemoglobin when oxygen is bound? When it is not bound? |
|
Definition
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|
Term
What molecule modulates Hb-O2 binding affinity? It also has an affinity for the deoxy form. |
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Definition
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|