Concept explainers
BIOCHEMICAL CONNECTIONS For the process
what are the signs of
Want to see the full answer?
Check out a sample textbook solutionChapter 1 Solutions
Owlv2,1 Term Printed Access Card For Campbell/farrell/mcdougal's Biochemistry, 9th
- REFLECT AND APPLY Design an experiment to purify protein X on an anion-exchange column. Protein X has an isoelectric point of 7.0.arrow_forwardBIOCHEMICAL CONNECTIONS We usually say that a perfect buffer has its pH equal to its pKa. Give an example of a situation in which it would be advantageous to have a buffer with a pH 0.5 unit higher than its pKa.arrow_forwardMATHEMATICAL Consider the reaction AB+C, where G=0.00. (a) What is the value of G (not G) when the initial concentrations of A, B, and C are 1 M, 103M,and106M? (b) Try the same calculations for the reaction D+EF, for the same relative order of concentrations. (c) Try the same calculations for the reaction GH, if the concentrations are 1Mand103M for G and H, respectively.arrow_forward
- REFLECT AND APPLY In which of the following processes does the entropy increase? In each case, explain why it does or does not increase. (a) A bottle of ammonia is opened. The odor of ammonia is soon apparent throughout the room. (b) Sodium chloride dissolves in water. (c) A protein is completely hydrolyzed to the component amino acids. Hint: For Questions 37 through 39, consider the equation G=HT(S).arrow_forwardMATHEMATICAL Using the information in Table 20.2, calculate G for the following reaction: 2Cytaa3[oxidized;Fe(III)]+2Cytb[reduced;Fe(II)]2Cytaa3[reduced;Fe(II)]+2Cytb[oxidized;Fe(III)]arrow_forwardMATHEMATICAL If a reaction can be written AB, and the G is 20kJmol1, what would the substrate/product ratio have to be for the reaction to be thermodynamically favorable?arrow_forward
- MATHEMATICAL For an enzyme that displays MichaelisMenten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? (a) [S]=KM (b) [S]=0.5KM (c) [S]=0.1KM (d) [S]=2KM (e) [S]=10KMarrow_forwardREFLECT AND APPLY Two biochemistry students are about to use mitochondria isolated from rat liver for an experiment on oxidative phosphorylation. The directions for the experiment specify addition of purified cytochrome c from any source to the reaction mixture. Why is the added cytochrome c needed? Why does the source not have to be the same as that of the mitochondria?arrow_forwardMATHEMATICAL You do an enzyme kinetic experiment and calculate a Vmax of 100 mol of product per minute. If each assay used 0.1 mL of an enzyme solution that had a concentration of 0.2 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol?arrow_forward
- REFLECT AND APPLY An amino acid mixture consisting of lysine, leucine, and glutamic acid is to be separated by ion-exchange chromatography, using a cation-exchange resin at pH 3.5, with the eluting buffer at the same pH. Which of these amino acids will be eluted from the column first? Will any other treatment be needed to elute one of these amino acids from the column?arrow_forwardMATHEMATICAL What is the ratio of TRIS/TRIS-H+ in a TRIS buffer at pH 8.7?arrow_forwardRECALL Using an energy diagram, show why the lock-and-key model could lead to an inefficient enzyme mechanism. Hint: Remember that the distance to the transition state must be minimized for an enzyme to be an effective catalyst.arrow_forward
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning