Busy. Please wait.

show password
Forgot Password?

Don't have an account?  Sign up 

Username is available taken
show password


Make sure to remember your password. If you forget it there is no way for StudyStack to send you a reset link. You would need to create a new account.

By signing up, I agree to StudyStack's Terms of Service and Privacy Policy.

Already a StudyStack user? Log In

Reset Password
Enter the associated with your account, and we'll email you a link to reset your password.

Remove ads
Don't know
remaining cards
To flip the current card, click it or press the Spacebar key.  To move the current card to one of the three colored boxes, click on the box.  You may also press the UP ARROW key to move the card to the "Know" box, the DOWN ARROW key to move the card to the "Don't know" box, or the RIGHT ARROW key to move the card to the Remaining box.  You may also click on the card displayed in any of the three boxes to bring that card back to the center.

Pass complete!

"Know" box contains:
Time elapsed:
restart all cards

Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.

  Normal Size     Small Size show me how

Biochemistry Final

UW-Platteville Buboltz's General Biochemistry Final Exam 2014 Fall

for amino acids with neutral R groups, at any pH below the pI of the amino acid, the population of amino acids in solution will have what charge a net positive charge
titration of valine by a strong base, for example NaOH, reveals two pK's. The titration reaction occurring at pK2 (pK2=9.62) is: -NH3 + OH- yields -NH2 + H2O
at the isoelectric pH of a tetrapeptide the total net charge is Zero
an enzyme is found to have a narrow range of pH within which it can function effectively. This pH range is centered around pH=5.7, & its catalytic activity is actually difficult to even measure just 2.2 pH units higher than this optimal value. Why? a conformational change occurs as the pH increases, which alters the protein's structure and therefore its function
for the amino acid lysine, the Henderson-Hasselbalch equation can be applied to how many ionization group(s) three
the primary structure of a protein specifically describes the linear sequence of its amino acids
the ionic charges associated with a protein molecule are mostly contributed by the side chains of constituent amino acids
a mixture of 5 proteins (X, Y, Z, N & Q) is applied to a size-exclusion column. Given the information supplied, which will elute third? (X-35,000, Y-26,000, Z-146,000, N-26,000, Q-14,000 in g/mol) Y and N elute together
the rate of migration for SDS-Page of polypeptides depends only on size and not on conformation
which of the following undergoes an oxidation reaction to form a disulfide bond? cysteine
a mutation that changes___________ would probably produce minimal effects on protein function, while a mutation that changes_________could produce dramatic effects LLe to Leu; Asn to Ala
which residue can function as a "pH sensitive molecular switch": histidine, cysteine, proline, serine, and methionine histidine
which of the following peptides would absorb light centered at 280 nm? ala-lys-his, his-pro-ala, ser-gly-asn, ala-ala-trp, or val-pro-leu ala-ala-trp; the aromatic amino acids absorb light around 280 nm
in an aqueous solution, a globular protein's conformation will always reflect the placement of hydrophobic residues within the interior of the protein
in the context of protein structure, which interactions are also known as "salt bridges" ionic bonds
how are side chains in the alpha-helix oriented radiate outward from the helical axis
amino acid residues commonly found in the middle of beta-turn are pro and gly
in a globular protein its tertiary structure is likely stabilized by the interactions of amino acid side chains in non-neighboring regions of the polypeptide chain
in a globular protein it could contain alpha helices that are stabilized by hydrogen bonds
in a globular protein it could contain disulfide bonds that stabilize its Tertiary structure
in a globular protein non-covalent forces are the primary source of stability for its secondary and tertiary structure
a scientist observes that protein X will fold into its native conformation only when protein Y is also present in the same solution. Protein Y, however, can fold into its native conformation without protein X being present. Therefore protein Y may be a molecular chaperone for protein X
in a protein the rotation about covalent bonds only can cause conformational changes
NMR is a technique that can be used to analyze the 3D-structure of proteins in solution
the polypeptide chains in the sheet are nearly fully extended in Beta-sheets
structures in beta-sheets can occur in both parallel and anti parallel forms
in anti parallel beta-sheets the hydrogen bonds between adjacent strands are nearly perpendicular to the backbones of the strands
adjacent strands in beta-sheets form hydrogen bonds within the plane of the sheet
Protein X can bind to either protein A or protein B to form a complex, with either association constant 10^8 M-1 (x with A) or 10^6 M-1 (X with B) which takes fewer molecules in the presence of excess X, it takes fewer molecules of A than B to generate a given amount of complex
about how many residues per turn of the alpha-helices 3.6
a coenzyme is something that is essential to the function of a protein, is not made up of amino acids, and is readily separated from the protein
an increase in blood pH will cause hemoglobin to bind more tightly to oxygen is a result of the effectors of hemoglobin-oxygen binding
conditions in the tissues which enhance the delivery of oxygen by hemoglobin are the presence of CO2, 2,3-BPG, and protons
which reversible reaction of carbon dioxide explains how hemoglobin serves as a transporter of CO2 reaction with the N-terminal amino groups to form a carbonate
a hyperbolic binding curve differs from a sigmoidal binding curve in that the hyperbolic curve implies one affinity state only (single Kd) for oxygen binding
in order to drive shape changes from the oxy form of hemoglobin to the deoxy form, attractive interactions must arise between oppositely charged groups on different subunits
an allosteric interaction between a ligand and a protein is one where binding of a molecule to a binding site affects properties of another site on the protein
a good transition-state analog binds to the enzyme more tightly than the substrate
which step in an enzyme-catalyzed reaction was assumed to be negligible by Michaelis and Menton in formulating their chemical model of enzyme action formation of ES from E + P
to calculate the turnover number of an enzyme, you need to know the enzyme concentration, and the initial velocity of the catalyzed reaction at [S]>>Km
what is the net charge on the peptide Gly-Ser-Arg-Lys-His-Asp-Val at pH 7.5? +1
what is the approximate molar mass of a protein containing 378 amino acids ~37,800
why do wool socks shrink when they are washed in hot water or heated in a dryer processed wool is rich in beta-sheets, but returns to native alpha-helices upon heating
what is the formula for a carbohydrate (CH2O)n
polysaccharide structure can be varied by differences in chain length (number of sugars in each polysaccharide), the kind(s) of sugars in each polysaccharides, the presence of branching, and the types of linkages between sugar units
what type of bond links the monomers of a polysaccharide glycosidic bond
sugar found in DNA adopts a 5-membered cyclic structure, is a deoxy form of ribose, has a D-configuration, and is bonded to phosphate via the 3' and 5' carbons
anomers can be interconverted via a linear intermediate
which does not apply to dihydroxyacetone: ketose, triose, chiral, water-soluble, or carbohydrate chiral
what is the most generic nucleic acid form for storing genetic information double-stranded DNA
in the Watson-Crick DNA model (i.e., "B-form" DNA), how many base pairs are found in one turn of the helix? 10
which base is at the 5' end of the molecule: ACCAGTCG A is at 5' end, G is at 3'
what base is only found in DNA thymine
what would be the effect of exposing both RNA and DNA to alkaline pH RNA is hydrolyzed to nucleoside monophosphates
Histones are proteins around which DNA must be tightly wound chromosomes. Therefore, one may infer that all 5 histone proteins are rich in _____residues, whose charges allow binding to the sugar-phosphate backbone of DNA lysine and arginine
it is easier to denature ("melt") DNA richer in AT than GC because there is one fewer hydrogen bond in an AT base pair
in the Watson-Crick model for the DNA double helix the two strands run anti-parallel to one another
in the Watson-Crick model for the DNA double helix the base-pairing occurs on the inside of the double helix
in the Watson-Crick model for the DNA double helix the double helix is what handed right-handed
in the Watson-Crick model for the DNA double helix the two strands have complementary sequences
in the Watson-Crick model for the DNA double helix the grooves are major and minor
storage fats that contain only saturated long chain fatty acids tend to form what at room temperature solids
what would you expect for the fatty acyl chains of the membrane phospholipids of bacteria grown at high temperature proportion of unsaturated fatty acyl groups decreases
the arrangement of lipid bilayers and other components is the basis for the currently widely accepted description which is called the fluid mosaic model
when red-blood cells are treated w/ globular proteases most are broken down into peptides but a small fraction of the protein content is resistant. If peptide cleavage is the only effect, how can the protease-resistant fraction be explained? it represents integral membrane proteins
fatty acids have an even number of carbon atoms between 16-24 in total
there are two types of lipids: non-polar lipids and "polar" lipids. Polar lipids are really just what amphiphatic
the shortest alpha helix segment in a protein that will span a membrane bilayer has about how many amino acid residues 20
individual lipid bilayer molecules are free to diffuse in what direction of the bilayer laterally in the surface of the bilayer
the fluidity of a lipid bilayer will be increased by increasing the temperature
G proteins act as signaling proteins but have a mechanism that does what that involves the hydrolysis of a nucleoside triphsphate intrinsic shut-off
which does not contribute to the regulation of enzymatic activity: protein phosphorylation, allosteric effectors, protein stability, mRNA stability, and DNA stability DNA stability
in the signal-cascade pathway that causes glucose to be released from glycogen in response to the hormone epinephrine, what is the immediate product of adenyl cyclase? cAMP
What are some similarities between transporters and enzymes undergo conformational changes upon binding their substrates, interact w/ their substrates stoichiometrically, reach a saturation limit when supplied w/ excess of substrate,& show structural complementarity in binding very specifically w/ their substrates
what is not a similarity between transporters and enzymes enzymes cause a chemical modification to their substrates; transporters just move them
in mitochondria, phosphate ion and H+ are transported together from the intermembrane space into the matrix. This means that the transport protein must be a symporter
citrate synthase is a key regulatory enzyme of the citric acid cycle. What are some inhibitors ATP, NADH
pyruvate kinase is allosterically inhibited by a high concentration of ATP
reaction steps that are far from equilibrium are good control points in metabolic pathways because these reactions are highly exergonig
F26BP does what to PFK-1 activates
F26BP does what to fructose-1,6-bisphosphate inhibits
is fructose-1,6-bisphosphatase reaction is exergonic or endergonic exergonic
why is it important for proper cll function that proteins turn over rather than persisting indefinately after being synthesized this would allow changes in enzyme activity levels. if proteins were never degraded, all enzymes wuld remain present indefinately
what happens to FBPase-2 when FBPase-2 is phosphorylated activated
what happens to PFK-2 when FBPase-2 is phosphorylated inactivated
what happens to [F26BP] when FBPase-2 is phosphorylated decrease
what happens to PFK-1 when FBPase-2 is phosphorylated inhibited
what happens to FBPase-1 when FBPase-2 is phosphorylated activated
what happens to glycolysis when FBPase-2 is phosphorylated slow down
what happens to gluconeogensis when FBPase-2 is phosphorylated will accelerate
which of these cofactors participates directly in most of the oxidation-reduction reactions in the fermentation of glucose to lactate?: ADP, ATP, FAD/FADH2, glyceraldehyde 3-phoosphate, or NAD+/NADH NAD+/NADH
the anerobic conversion of 1 mol of glucose to 2 mol of lactate (i.e., no citric acid cycle, no ox-phos) is accompnaied by a net production of how much ATP 2 mol of ATP
the conversion of 1 mol of pyruvate to 3 mol of CO2 via pyruvate dehydrogenase and the citric acid cycle also yields 4 mol of NADH, 1 mol of FADH2, and 1 mol of ATP (or GTP)
the rate of entry of acetyl-CoA into the citric acid cycle is decreased when the ratio of [ATP]/[ADP] is high
citrate synthase and the NAD+-specific isocitrate dehydrogenase are two key regulatory enzymes of the citric acid cycle. These enzymes are inhibited by: ATP and/or NADH
reducd QH2 is not formed by which complex complex III and cytochrome c
almost all of the xygen (O2) one consumes in breathing is converted to water
Vitamin B2 (riboflavin) FAD
Vitamin B1 TPP; thiamine pyrophosphate
Vitamin B3 NAD+
Vitamin B5 Coenzyme A
complex I is NADH: ubiquinone oxido reductase
Complex II is succinate dehydrogenase
Complex III is cytochrome bc1 complex
Complex IV is cytochrome oxidase
Created by: 530848841