How does NH4SO4 affect water structure? Whatdoes this have to do with protein solubility?I thought the answer was that NH4S04 attractsH2O so the protein doesn't bind to H2Oallowing the protein to bind to each other. Butthe answer given is, orders water locally tobecome more ice-like.Can someone explain?

One of the factors that determine the solubility of proteins in solution is the concentration of…

Answered: How does NH4SO4 affect water structure?…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Explain the use of passing the inside-out vesicles contaminated with right-side-out vesicles through the affinity column made of lectin coupled to solid beads.
4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…
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The molecule that condensed with a phosphate group to form the head group of the lipid shown in the first image (picture 6) is choline, an essential component of many cellular molecules. (a) Draw the structure of choline and explain why it needs a transport protein in order to enter cells. (b) Cells must transport choline from outside the cell (where it is relatively rare) to the inside of the cell (where it is relatively abundant). The diagram below represents a cell with a choline transporter (labeled T). Draw a solid arrow through the transporter to show the direction in which choline travels (into or out of the cell). (c) Is T an active or passive transport protein for choline? (d) For every choline molecule that moves through T, a sodium ion moves through the same transport protein at the same time. The sodium ion moves down its gradient. Add a dashed arrow to the diagram in part (b) to show the direction of movement of sodium. (e)…
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Saccharide X, a sugar composed of repeating cellobiose and maltose, is a constituent of two glycoproteins, which are receptors that are found in a certain membrane. For the first glycoprotein, the saccharide is linked by a(1-2) linkages to three sialic acid residues, then O-linked to the glycoprotein. The other glycoprotein, on the other hand, has the saccharide linked by a B(1-3) bond also to three sialic acid residues, then also O-linked to the glycoprotein. The saccharide was cleaved from its sialic acid residues. The treatments and results are as follows: 1. hydrolysis by B(1-> 4) - disaccharide products 2. hydrolysis by a(1-> 4) - release of 2 disaccharide & 2 monosaccharide units. Show the structure of the saccharide.
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
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How does NH4SO4 affect water structure? What does this have to do with protein solubility? I thought the answer was that NH4S04 attracts H2O so the protein doesn't bind to H2O allowing the protein to bind to each other. But the answer given is, orders water locally to become more ice-like.