BIOCHEMISTRY-ACHIEVE (1 TERM)
9th Edition
ISBN: 9781319402853
Author: BERG
Publisher: MAC HIGHER
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Question
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-ACHIEVE (1 TERM)
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. 29PCh. 3 - Prob. 30PCh. 3 - Prob. 31P
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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_forwardIn terms of structure and function of a protein why is the lactase enzyme have a optimal pH of sevenarrow_forwardFigure 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_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_forwardIs this the correct answer of R and T in the blanks or are they switched?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
- Are all the amino-acids soluble in water? Explain why?arrow_forwardWhich 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_forward
- Suggest a reason why amino acids are usually more soluble at pH extremes than they are at neutral pH. (Note: This does not mean that they are insoluble at neutral pH).arrow_forwardA cytosolic protein has an important alpha amino group. The pKa of this group is approximately 8 when exposed to water outside of a protein. 1. What would happen to the pKa if this group was instead buried in the hydrophobic interior of the protein? Explain. 2. Let’s say in the hydrophobic interior of the protein, the group forms an ionic bond with a carboxylate group of the side chain of a charged Asparagine residue. How would the pKa of this alpha amino group compare with the pKa of the alpha amino group in the hydrophobic interior of the protein without a nearby Asparagine residue to form this ionic bond? Explain.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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