Modified Mastering Chemistry with Pearson eText -- Standalone Access Card -- for Biochemistry: Concepts and Connections
1st Edition
ISBN: 9780133882797
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Textbook Question
Chapter 2, Problem 14P
What is the molecular basis for the observation that the overall charge on a protein becomes increasingly positive as pH drops and more negative as pH increases?
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Chapter 2 Solutions
Modified Mastering Chemistry with Pearson eText -- Standalone Access Card -- for Biochemistry: Concepts and Connections
Ch. 2 - Suppose a chloride ion and a sodium ion are...Ch. 2 - Draw two different possible hydrogen-bonding...Ch. 2 - Prob. 3PCh. 2 - 4. What is the pH of each of the following...Ch. 2 - Prob. 5PCh. 2 - The weak acid HA is 2% ionized (dissociated) in a...Ch. 2 - 7. Calculate the pH values and draw the titration...Ch. 2 - What is the pH of the following buffer mixtures?...Ch. 2 - a. Suppose you wanted to make a buffer of exactly...Ch. 2 - Prob. 10P
Ch. 2 - You need to make a buffer whose pH is 7.0, and you...Ch. 2 - Describe the preparation of 2.00 L of 100 glycine...Ch. 2 - Carbon dioxide is dissolved in blood (pH 7.4) to...Ch. 2 - What is the molecular basis for the observation...Ch. 2 - The anno acid arginine ionizes according to the...Ch. 2 - It is possible to make a buffer that functions...Ch. 2 - A student is carrying out a biological preparation...Ch. 2 - Histidine is an amino acid with three titratable...Ch. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21P
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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
- Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.arrow_forwardHow many charged functional groups will be found on serine at physiological pH?arrow_forwardWhy is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?arrow_forward
- The interactions between the 2 a and 2 b subunits of hemoglobin represent what type of protein structure?arrow_forwardMost protein dissolve in neutral salt solution, is that true? Provide reasoningarrow_forwardWhat is the net average charge on the predominant form of lysine at pH values of (a) 2.0, (b) 5.0and (c) 7.0?arrow_forward
- Are peptide bonds free to rotate in folded protein? Can they be ionized at extreme pH values?arrow_forwardBased on molecular weights of purified (no beta-Me) and (beta-Me) sample, which are 140 kDa and 72 kDa, what can be said about the number and size of the protein monomers, as well as the nature of the bonds holding together the complete quaternary structure of the proteins?arrow_forwardWhat is the net charge on the peptide RHTLE at pH 12.5?arrow_forward
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