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Biochem Review (all 120 cumulative questions)

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Name an organelle only found in animal cells
What direction would you expect glucose to rotate polarized light?
Name the amino acid that has a guanidinium group.
Name the compound used in amino acid analysis to color amino acids
What is the net charge of Histidine at pH 1?
Name the organelle that allows plants to convert lipid to carbohydrate.
Name the reagent that breaks peptide bonds at the N-terminal of aromatic amino acids.
Name an organelle in an animal cell other than the nucleus that contains DNA.
Name the term for a molecule that is both hydrophobic and hydrophilic.
What is the number of fragments obtained from the enzymatic interaction of the peptide A-G-T-R-D-T-A-S-K-E-L with trypsin?
What is the number of fragments obtained from the enzymatic interaction of the peptide A-G-T-R-D-T-A-S-K-E-L with chymotrypsin?
What compound converts methionine to homoserine lactone?
What type of column procedure would best separate proteins from peptides?
Name the enantiomer for D-Glucose.
Name a hydroxylated amino acid with 4 stereoisomers.
If an individual had a [.21M] concentration of bicarbonate ion and a [.02M] concentration of carbonic acid, how might this effect the physiologic pH of their blood?
What is the proton concentration of a solution with a pH of 4?
What is the net charge of A-G-T-R-D-T-A-S-K-E-L at physiologic pH?
What is the net charge of glutamic acid at physiologic pH?
To the nearest whole number, what is the isoelectric point of glutamic acid?
What type of secondary structure of proteins has intra-chain H-Bonds?
What type of chromatography utilizes ligands?
To the nearest tenth, at what specific pH could you best precipitate most amino acids?
What is the estimated molecular weight of a 22 amino acid peptide?
If amino acid analysis provides a ration of 2G:Y:4H, and you know the MW is 1700, how many amino acids are in your sample?
What is the name of the cell structure of bacteria that protect it from hypotonic solution?
Name the amino acid with an imidazole group.
If the R-groups of valine and proline were close in space, name the type of interaction they might share.
If the R-groups of arginine and lysine were close in space, name the type of interaction they might share.
If the R-groups of glutamine and threonine were close in space, name the type of interaction they might share.
Casein is a storage protein, what does it store?
Name a destructive technique that can assist in the assessment of purity, molecular weight, size and charge of a compound.
Name a compound that utilizes florescence to identify the N-terminal amino acid.
Name the technique that produces PTH-derivatives.
In an alpha helix, how many amino acids are present per turn?
Name the unique property of water that describes why we feel cold when coming out of a hot shower.
What happens to the pKa of a molecule when it is in a strong acid?
At what minimum pH would you expect that Sanger’s reagent to NOT be able to bind to the R-group of lysine. (whole #)
The abbreviation GLX from amino acid analysis indicates the presence of THIS amino acid.
If amino acid analysis indicated the presence of methionine, but cyanogen bromide produced no peptide cleavage, what would you know about the peptide?
Provide the glycosidic linkage for lactose.
Name the enzyme class that requires ATP.
Name an inhibitor molecule that could covalently bind to a serine protease.
Name the non-protein part of the holoenzyme.
Aspartame contains aspartic acid and what other amino acid?
What is the velocity of a reaction that has a substrate concentration equal to 0.5 times the Km?
On a Line-Weaver Burke plot, what is the s the x-intercept if the Vmax=3 and the Km=2?
Name the protomers unique to fetal hemoglobin.
Name the molecule that reduces hemoglobin’s affinity for oxygen.
Name a heteropolysaccharide.
What is the product of hydrogenation of oleic acid?
What is the oxygen pressure in the capillaries?
How many carbon dioxide binding sites does hemoglobin have?
Any molecule or pathogen capable of eliciting an immune response is called this.
Name the type of immune system that utilizes killer T-cells.
Name the term for an enzyme that takes on different forms within an organism.
Name given to an inactive precursor of an active enzyme.
Name the enzyme that makes the product pi-chymotrypsin.
How many amino acids are found in the active chymotrypsin molecule?
List the other name for Product 2 upon chymotrypsin enzymatic cleavage.
List the catalytic triad components of trypsin including their number in the primary sequence.(ex. Ala94-Arg567-Met3)
What is the major product created in the secondary process of photosynthesis?
Try to name a 5-carbon carbohydrate that has a ketone group.
Alpha-D-Glucose has carbon number four’s –OH group pointing in this direction.
The inter-conversion between the alpha and beta forms in solution is referred to as this term.
List the two carbon numbers on either side of oxygen for the closed ring structure of fructose.
What is the anomeric carbon number for aldohexose?
Extensin contains a lot of this amino acid
Name an anticoagulant polysaccharide.
Polysaccharide providing rigidity to exoskeletons.
Type of polysaccharide created by the partial hydrolysis of starch.
Sulfa drugs utilize this type of inhibition.
Name the malaria-causing protozoan.
Name two enzymes that evolved convergently.
Name a fatty acid with an 18:2 abbreviation.
Name a lipoprotein that has about 50% cholesterol.
Name a disease resulting from a deficiency of GM2 Gangliosidase.
Name the amino acid N-linked carbohydrate is attached to.
Name a bile salt.
Why is it called the “fluid” mosaic model of membranes?
Fat digestion begins in what part of the human body?
Name the enzyme that covalently attaches cDNA to the original plasmid.
Name a fat-soluble vitamin provided by intestinal bacteria.
Name the enzyme needed to synthesize DNA.
Name of the endoplasmic reticulum receptor that recognizes a newly translated protein.
Would you expect the amino acid that a (A-G-U) DNA code would transcribe to be hydrophobic?
Name the cofactor for thiamine.
Name the cofactor for vitamin B2.
What is the one letter code for the essential amino acids.
How many Calories in a pound of fat?
List the three essential fat-soluble vitamins.
What is the vitamin form for the pre-vitamin 7-dehydrocholesterol?
Name antagonist to vitamin K.
Name the anti-beriberi factor.
What is the vitamin for the cofactor NAD+?
What vitamin deficiency causes pellagra?
Name the vitamin that forms coenzyme A.
What is the nucleotide that AZT competes with?
Name the dehydrated form of Watson-Crick DNA.
Name the RNA in the lowest concentration.
Where does the amino acid bind to the tRNA?
In the pre-priming step what is the protein that binds to the lagging strand?
What is the enzyme that binds the lagging strand complementary fragments?
What is the term that describes tRNA leaving the ribosome after it drops off an amino acid?
Name a modified nitrogenous base.
Name a term to describe the first 15-30 hydrophobic amino acids of a newly translated protein.
Name the enzyme to cleave the plasmids used for bioengineering of E. Coli.
Term for transplanting a nucleus of a donor adult cell to an egg with a removed nucleus.
Diagnostic tests detecting different sized DNA fragments when cleaved by a restriction enzyme.
Disease resulting from missing the enzyme to convert tyrosine to melanin.
Name for a set of genes in bacteria that work in concert.
What is the DNA code that codes for the peptide MET-TRP.
Name the protein that prevents the re-annealing of DNA strands during DNA replication.
Disease resulting from the missing enzymes responsible for a deficiency in excision and repair.
Most higher animals can synthesize this vitamin from glucose.
Deficiencies in this mineral could result in an endemic goiter.
The term for molecules capable of self-replication.
Term for the compound that regulates gene expression by turning off of genes.
The type of mutation that involves the addition of nucleotides to existing DNA.
The term for a sugar attached to a nitrogenous base.

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