Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
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Chapter 3, Problem 6P
Interpretation Introduction
Interpretation:
The reason for the precipitation of proteins at high salt concentrations and some of them require salt to dissolve in water should be determined.
Concept introduction:
A peptide bond exists between the two amino acids. During the formation of a peptide bond, a molecule of water is released. The carboxyl group of one amino acid gets linked with the amino group of the other amino acid. Polypeptides and proteins are the chains formed by the amino acids.
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Chapter 3 Solutions
Biochemistry
Ch. 3 - Prob. 1PCh. 3 - Prob. 2PCh. 3 - Prob. 3PCh. 3 - Prob. 4PCh. 3 - Prob. 5PCh. 3 - Prob. 6PCh. 3 - Prob. 7PCh. 3 - Prob. 8PCh. 3 - Prob. 9PCh. 3 - Prob. 10P
Ch. 3 - Prob. 11PCh. 3 - Prob. 12PCh. 3 - Prob. 13PCh. 3 - Prob. 14PCh. 3 - Prob. 15PCh. 3 - Prob. 16PCh. 3 - Prob. 17PCh. 3 - Prob. 18PCh. 3 - Prob. 19PCh. 3 - Prob. 20PCh. 3 - Prob. 21PCh. 3 - Prob. 22PCh. 3 - Prob. 23PCh. 3 - Prob. 24PCh. 3 - Prob. 25PCh. 3 - Prob. 26PCh. 3 - Prob. 27PCh. 3 - Prob. 28PCh. 3 - Prob. 29P
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- Proteins are thermodynamically unstable. The ΔG of the hydrolysis of proteins is quite negative, yet proteins can be quite stable. Explain this apparent paradox. What does it tell you about protein synthesis?arrow_forwardMost protein dissolve in neutral salt solution, is that true? Provide reasoningarrow_forwardIn terms of structure and function of a protein why is the lactase enzyme have a optimal pH of sevenarrow_forward
- Figure 7 shows one additional type of bond that can stabilize the tertiary structure of a protein. This bond is called a disulfide bond (or disulfide bridge), and it involves the sulfhydryl (-SH) R groups from one particular type of amino acid. A disulfide bond can form only under certain conditions (oxidative conditions). We'll talk about oxidation and reduction next week. For now, just note that this type of bond does exist in some proteins. Answer the below questions on tertiary structure in your own document. 8. Figure 6 shows examples of bonds that might stabilize the tertiary structure of a protein (labeled A, B, and C). Do these interactions involve only the amino acid R groups, only the polypeptide backbone atoms, or both? 9. In the table below, indicate what type of bond/ interaction is represented in the examples shown in Figure 6, panels A, B, and C and whether each interaction involves group or backbone atoms. Example Type of Bonding Interaction R group or backbone? A В 10.…arrow_forwardHow can a protein’s potential function be determined from a protein’s primary structure? I assumed this was not possible, I thought its function was determined from its 3-dimensional structure only. Thank you for explaining this.arrow_forwardAt low salt concentration, proteins are less solublearrow_forward
- Proteins such as enzymes can be denatured by high temperatures or environments with extreme pH deviations making them unable to function. How do these conditions make proteins nonfunctional?arrow_forwardWhich intermolecular forces are important in acetic acid, CH3 –(C=0)-oh? A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the inside or the outside of the folded protein? Briefly explain. The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.arrow_forwardThe pKa of an acid depends partly on its environment. Predict the effect of each of the following environmental changes on the pKa of a glutamic acid side chain. (a) A lysine side chain is brought into proximity. (b) The terminal carboxyl group of the protein is brought into proximity. (c) The glutamic acid side chain is shifted from the outside of the protein to a nonpolar site insidearrow_forward
- Which of the following amino acids would you least expect to find on the surface of a water-soluble protein? Explain I Serine Glutamat Lysime Threoninearrow_forwardRelatively hydrophobic proteins will require higher amounts of (NH4)2S04 to precipitate.arrow_forwardIn an experiment attempting to explain how proteins act and denaturation, an egg white was used and full cream milk in heating from a sauce pan. Why is it not recommended to use reconstituted or evaporated milk? Why is full cream milk suggested to be used?arrow_forward
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