Dideoxycytidine tri-phosphate cannot be incorporated into growing DNA chains.
Dideoxycytidine is an analog of the nucleoside deoxycytidine.
Dideoxycytidine tri-phosphate is used to terminate DNA chain elongation during DNA sequencing.
Dideoxycytidine has hydrogen groups on the 2’- and 3’-carbons of deoxyribose.
Dideoxycytidine is converted to a nucleoside tri-phosphate by cellular kinases.
Alters the specificity of the sigma factor of RNA polymerase.
Prevents the binding of RNA polymerase to promoters.
Increases the affinity of CAP for cAMP.
Decreases the affinity of CAP for cAMP.
Causes CAP to bind constitutively to CAP-binding sites.
Peroxisomes, Rough Endoplasmic Reticulum
Lipid Droplets, Smooth Endoplasmic Reticulum
Mitochondrion, Smooth Endoplasmic Reticulum
Lysosomes, Golgi Apparatus
Phosphorylation of amino acid side chains
Proteolytic cleavage of peptide bonds within the zymogen
Degradation of the enzyme
Converting activated enzymes to zymogens
This amino acid residue can form disulfide bonds under oxidizing conditions.
This residue can adopt a cis conformation of the peptide bond within a protein.
The side chain of this amino acid has multiple atoms that can participate in hydrogen bonds.
The side chain of this amino acid is positively charged at physiologic pH.
This amino acid can serve as an attachment site for O-linked polysaccharides (sugars) in glycoproteins.
Failure to inhibit gastric lipase
Excess undigested fats
Accumulation of Orlistat in the intestinal tract
Non-specific inhibition of many enzymes
His blood pressure of 135/82 identifies him as risk for hypertension
His BMI places him in the “normal” range
We should repeat the a1C and order a fasting plasma glucose (FPG) test on a non-urgent basis
His blood pressure is within the “normal” range
His hemoglobin a1C level of 6.2% identifies him as at increased risk of diabetes
Nitric oxide (NO) is released from Hb preferentially at sites of active metabolism, because a cysteine has a much higher affinity for NO in oxyhemoglobin than in deoxyHb.
Hemoglobin and myoglobin molecules can bind 2,3-bisphosphoglycerate, which decreases their affinity for oxygen.
Carbon dioxide increases the affinity of hemoglobin for oxygen both by binding to the N-terminus and through the Bohr effect.
The Hill Coefficient of hemoglobin indicates that hemoglobin tetramers have no more than three oxygen molecules bound.
Sites of active metabolism have higher concentration of carbonic acid, which shifts the hemoglobin oxygen dissociation curve to the left.
Gave them hydroxyurea to increase the synthesis of HbF.
Had them ingest a reducing agent to regenerate the oxygen binding form of Hb.
Gave them hydroxyurea to increase the synthesis of HbF.
Administered air with a higher percent of carbon dioxide than is normal, to compete with the carbon monoxide.
Administered 100% oxygen to displace the competitive inhibitor.
In going from a pO2 of 20mmHg to a pO2 of 100mmHg, stripped Hb takes up about three times as much oxygen as does Hb from whole blood, per mole of tetramer.
In going from a pO2 of 100mmHg to a pO2 of 20mmHg, Hb from whole blood releases about three times as much oxygen as does stripped Hb, per mole of tetramer.
The P50 value for stripped Hb is ~ 40mmHg lower than that for whole blood.
The P50 value for stripped Hb is ~ 15mmHg higher than that for whole blood.
Changing the pH would not affect the oxygen saturation curve of the stripped Hb.
Depends on the differing reactivity of the R and T forms of Hb
Leads to decreased blood flow at tissue sites with low oxygen pressure.
Can competitively inhibit cyanide poisoning.
Competes with carbon dioxide binding.
Is mediated by formation of C?-CH2-S-NO bond with Met.
Glucose 6-phosphate and enzyme E
Creatine phosphate and enzyme A
A vast excess of ATP
Pyrophosphate and enzyme D
Coupling of the synthesis of ATP to the reaction.
Enzyme catalysis of the reaction.
Generation of a higher temperature by the cell.
Coupling of ATP hydrolysis to the reaction.
Transfer of a phosphate group from the substrate to ADP.
Base + sugar + phosphate --> nucleotide
N2 + H2 --> ammonia
Sucrose --> CO2 + H2O
CO2 + H2O --> sugar
Amino acid + amino acid --> peptide
Disruption of the inner mitochondrial membrane stops ATP formation.
Complex I can only react with NADH from the matrix side while complex III can only reduce cytochrome c from the intermembrane space.
A pH gradient is set up across the inner mitochondrial membrane, with the pH higher in the matrix.
At least one component of each major electron transport complex is coded for by mt DNA.
Oxidation-reduction reactions of the electron transport chain generate a gradient of protons across the inner mitochondrial membrane.
A decrease in the cytosolic concentration of ADP.
A decrease in the activity of mitochondrial outer membrane transport proteins.
An increase in mitochondrial AMP.
An increase in mitochondrial ATP production.
A decrease in the cytosolic concentration of ATP.
The reduction of one NAD+.
The net consumption of one oxaloacetate.
The net synthesis of one citrate.
The production of six ATPs.
The release of two CO2.
CoA, lipoic acid, biotin and ATP
CoA, ATP, NAD+ and riboflavin
CoA, thiamine pyrophosphate and folic acid
CoA, lipoic acid, thiamine pyrophosphate and FAD
An event or exposure that occurs more often in people with a disease than without
An event, condition, or characteristic that plays an important role in disease occurrence..
An event that precedes the onset of a disease
A hazard or exposure that occurs in workplaces where people get sick.
All of the above
The bacterial genome shows a defect in lagging strand DNA chain elongation.
The bacterial genome shows a defect in mismatch repair.
The bacterial genome shows accumulation of telomeric repeats.
The bacterial genome shows a defect in the removal of RNA primers.
The bacterial genome shows an increased number of replication errors.
Transposons may either activate or inactivate a gene.
In transposition, both the donor and target sites must be homologous.
Integration of human immunodeficiency virus (HIV) in the human genome occurs via a “transposition-like” mechanism.
Transposons have “insertion sequences” that are recognized by transposase.
Transposons can move from one location to a different one within a chromosome.
Kinesins and dynein can move on the same structure.
The “power stroke” occurs when the products of hydrolysis are released.
All three classes of motors are ATPases.
Dynein moves on microtubules towards the centrosome.
When the subunit at the + end of the polymer is NTP, the end is more stable than if the nucleotide is NDP.
The energy of NTP hydrolysis is required for polymerization.
The nucleotide in the subunit at the end of the polymer affects the equilibrium constant of subunit addition at the end.
NTP hydrolysis occurs after polymerization.