Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Videos
Textbook Question
Chapter 18.4, Problem 18.1CIAP
The proteins collagen, bovine insulin, and human hemoglobin have isoelectric points of 6.6, 5.4, and 7.1, respectively. Suppose a sample containing these proteins is subjected to electrophoresis in a buffer at pH 6.6. Describe the motion of each with respect to the positive and negative electrodes in the electrophoresis apparatus.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
A galvanic cell at a temperature of 25.0 °C is powered by the following redox reaction:
2+
2+
Sn(aq) +Ba(s) → Sn (s) + Ba** (aq)
2+
2+
Suppose the cell is prepared with 7.71 M Sn in one half-cell and 5.89 MBa in the other.
Calculate the cell voltage under these conditions. Round your answer to 3 significant digits.
Suppose you wish to sediment a sample of spherical protein molecules (molar mass
of 98.1 kg/mol and radius 3.40x10-9 m) in a liquid using a centrifuge. The sample is
placed 5.0 cm from the centrifuge's axis of rotation and is rotated at 6000 Hz.
a) What is the centripetal acceleration (i.e. the "g") the sample experiences from the
centrifuge?
b) If the liquid has a density of 900 kg/m3 and the terminal velocity of the protein is
4.10x10 6 m/s, what is the viscosity of the liquid?
Which of the following options shows the correct order of fastest to slowest motion of chloride ions, glycine and proteins through the separating gel?
Chloride ions > Proteins > Glycine
Glycine > Chloride ions > Proteins
Chloride ions > Glycine > Protein
Protein > Chloride ions > Glycine
You are trying to separate a mixture of AMP, ADP, and ATP using ion exchange chromatography. Select appropriate supplies for your experiment.
A positively charged column, deprotonated buffer, NaCl of same concentration.
A positively charged column, protonated buffer, NaCl of increasing concentration.
A negatively charged column, protonated buffer, NaCl of increasing concentration
You cannot separate nucleotides using ion exchange chromatography.
Chapter 18 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 18.2 - Prob. 18.1PCh. 18.2 - Prob. 18.2PCh. 18.3 - Prob. 18.3PCh. 18.3 - Examine the ball-and-stick model of valine in the...Ch. 18.3 - Indicate whether each of the following molecules...Ch. 18.3 - Prob. 18.6PCh. 18.3 - Prob. 18.7KCPCh. 18.3 - Prob. 18.8PCh. 18.3 - Prob. 18.9PCh. 18.3 - Prob. 18.10P
Ch. 18.3 - Prob. 18.11PCh. 18.3 - Prob. 18.12PCh. 18.4 - The proteins collagen, bovine insulin, and human...Ch. 18.4 - Prob. 18.2CIAPCh. 18.4 - Prob. 18.13PCh. 18.4 - Prob. 18.14PCh. 18.5 - Valine is an amino acid with a nonpolar side...Ch. 18.5 - Tripeptides are composed of three amino acids...Ch. 18.5 - Prob. 18.17PCh. 18.5 - Identify the amino acids in the following...Ch. 18.5 - Prob. 18.19PCh. 18.5 - Prob. 18.3CIAPCh. 18.5 - Prob. 18.4CIAPCh. 18.5 - Two of the most complete (balanced) proteins...Ch. 18.6 - Prob. 18.6CIAPCh. 18.6 - Prob. 18.7CIAPCh. 18.6 - (a)What atoms are present in a planar unit in a...Ch. 18.6 - Prob. 18.21PCh. 18.6 - Prob. 18.22PCh. 18.7 - Prob. 18.23PCh. 18.7 - Prob. 18.24PCh. 18.7 - Complete the following two sentences with either...Ch. 18.7 - Prob. 18.26KCPCh. 18.8 - Which of the following pairs of amino acids can...Ch. 18.8 - Look at Table 18.3 and identify the type of...Ch. 18.8 - In Figure 18.3, identify the amino acids that have...Ch. 18.8 - Prob. 18.30PCh. 18.9 - Prob. 18.31PCh. 18.10 - Another endoprotease is trypsin. Trypsin...Ch. 18.10 - Prob. 18.33PCh. 18.10 - Prob. 18.8CIAPCh. 18.10 - Prob. 18.9CIAPCh. 18 - Draw the structure of the following amino acids,...Ch. 18 - Prob. 18.35UKCCh. 18 - Prob. 18.36UKCCh. 18 - Prob. 18.37UKCCh. 18 - Prob. 18.38UKCCh. 18 - Threonine has two chiral centers. Draw L-threonine...Ch. 18 - Name four biological functions of proteins in the...Ch. 18 - Prob. 18.41APCh. 18 - Prob. 18.42APCh. 18 - Prob. 18.43APCh. 18 - Prob. 18.44APCh. 18 - Prob. 18.45APCh. 18 - Prob. 18.46APCh. 18 - Prob. 18.47APCh. 18 - Draw leucine and identify any chiral carbon atoms...Ch. 18 - Prob. 18.49APCh. 18 - Prob. 18.50APCh. 18 - Is histidine hydrophilic or hydrophobic? Explain...Ch. 18 - Prob. 18.52APCh. 18 - At neutral pH, which of the following amino acids...Ch. 18 - Prob. 18.54APCh. 18 - Prob. 18.55APCh. 18 - Prob. 18.56APCh. 18 - Prob. 18.57APCh. 18 - Proteins are usually least soluble in water at...Ch. 18 - Prob. 18.59APCh. 18 - Prob. 18.60APCh. 18 - Prob. 18.61APCh. 18 - Prob. 18.62APCh. 18 - Prob. 18.63APCh. 18 - (a)Identify the amino acids present in the peptide...Ch. 18 - Prob. 18.65APCh. 18 - Prob. 18.66APCh. 18 - Prob. 18.67APCh. 18 - Prob. 18.68APCh. 18 - Prob. 18.69APCh. 18 - Prob. 18.70APCh. 18 - Prob. 18.71APCh. 18 - Prob. 18.72APCh. 18 - Prob. 18.73APCh. 18 - Prob. 18.74APCh. 18 - Prob. 18.75APCh. 18 - What kind of bond would you expect between chains...Ch. 18 - Is the bond formed between each pair in Problem...Ch. 18 - Prob. 18.78APCh. 18 - Prob. 18.79APCh. 18 - Prob. 18.80APCh. 18 - Prob. 18.81APCh. 18 - Prob. 18.82APCh. 18 - Prob. 18.83APCh. 18 - Prob. 18.84APCh. 18 - Prob. 18.85APCh. 18 - Prob. 18.86APCh. 18 - Prob. 18.87APCh. 18 - Prob. 18.88APCh. 18 - Give an example of a protein that has quaternary...Ch. 18 - Prob. 18.90APCh. 18 - Prob. 18.91APCh. 18 - Prob. 18.92APCh. 18 - Prob. 18.93APCh. 18 - Prob. 18.94APCh. 18 - Prob. 18.95APCh. 18 - Prob. 18.96APCh. 18 - Prob. 18.97APCh. 18 - Prob. 18.98CPCh. 18 - Prob. 18.99CPCh. 18 - Prob. 18.100CPCh. 18 - Prob. 18.101CPCh. 18 - Prob. 18.102CPCh. 18 - Prob. 18.103CPCh. 18 - Prob. 18.104CPCh. 18 - Prob. 18.105CPCh. 18 - Prob. 18.106CPCh. 18 - Prob. 18.107CPCh. 18 - Prob. 18.108CPCh. 18 - Prob. 18.109GPCh. 18 - Prob. 18.110GPCh. 18 - Prob. 18.111GPCh. 18 - Prob. 18.112GP
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Instead, you decide to use ion exchange chromatography to further purify -galactosidase away from other proteins in your sample. You first run an anion exchange column equilibrated using column buffer with a pH of 5.0. a. What charge does the matrix of an anion exchange column have? b. Explain your answer in one or two complete sentences.arrow_forwardPhosphate buffered saline (PBS) is a very common reagent in cell biology labs that do cell culture since is it osmotically stable for most eukaryotic cells. It is often prepared as 10X PBS (10.5 mM KH2PO4, 1.552 M NaCl, 29.7 mM Na2HPO4) to save on shelf space. How would you prepare 1 L of 10X PBS given 1M KH2PO4, NaCl (FW 58.44), 906mM Na2HPO4? What is the concentration of each component in 1X PBS? How would you prepare 750 ml of 1X PBS?arrow_forwardThe α-amylase (α-AM) enzyme secreted by Aspergillus has an isoelectric point of approximately 4.2. If the purification method in problem 1 operates at pH 6.5, would the protein carry a positive charge, negative charge, or net zero charge?arrow_forward
- a Mixtureof the following amino acids is subjected to paper electrophoresis: Gly, Arg and Asp.Which of these amino acids will at (a) pH 2.0 and (b) pH 10 move to the Anode (+) and which will move to the cathode(-)? Motivate your answer.arrow_forwardWhat is the water potential (Ψ) of a 0.2 M sucrose solution in an open water bath at 20 °C?arrow_forwardThe CMC of SDS is 8.2 mM at 25 °C. Please describe the biological membrane solubilization when [SDS] is below or above 8.2 mM in the solution.arrow_forward
- A chemistry student at GGC synthesized a new sulfonamide (S7) drug to help treat malaria. Using a spectrophotometer the student observed that S7 converts to a colorless molecule in the presence of malaria parasite called Plasmodium falciparum. To study the rate of reaction, the student recorded the absorbance/amount of S7 at a wavelength of 570 nm. The results are summarized in the table below: Time (s) Absorbance/Amount of S7 0.80 0.63 10 0.50 15 0.40 20 О.32 25 0.25 30 0.20 Determine the half-life of S7. Include units in your answer MacBook Air 000 000 F8 80 F7arrow_forwardin food microbiology, how do you compute for concentration (M) and absorbance (A) of peroxidase activity on hydrogen peroxide at different pH values? (wavelength used = 415nm). can you please explain the calculations thank you if given: Temperature = 75 C Molar absorptivity coefficient = 10.5 Path length (cm) = 2 I = transmitted light = 0.45arrow_forwardIf you were given the task of determining the approximate % solute of potato cells. You decide to set up a series of 10 cups ranging from dH2O to 1% sucrose solution. You intend to drop a potato stick in each cup. a. What data would I need to collect for each potato stick? b. Why would I need to look for the solutions that have no effect on the potato stick?arrow_forward
- Please note when values are sourced from an appendix/table. Include any assumptions.arrow_forwardWrite the RHR, OHR, and the balanced overall reaction of the voltaic cell. To determine OHR and RHR, look at the columns labeled as Anode and Cathode.arrow_forwardA spheroidal bacterium with a diameter of 1.0 μm (micrometer, 1 μm = 10-6) contains 25,000 molecules of the protein hexokinase. What is the molar concentration of the protein inside the cell?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
GCSE Chemistry - Acids and Bases #34; Author: Cognito;https://www.youtube.com/watch?v=vt8fB3MFzLk;License: Standard youtube license