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

See similar textbooks

Similar questions

Transport of histidine into a bacterial cell was measured at several different histidine concentrations, see table below. Based on these data, is histidine uptake facilitated by a carrier or channel protein? a b Histidine (uM) 2.5 7 16 31 72 с Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. A carrier protein because it becomes saturated. A carrier protein because it does not become saturated. A channel protein because it becomes saturated. Transport (uM/min) d A channel protein because it does not become saturated. 42.5 119 240 490 1000 X Your answer
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.…
What amino acids can be found in chymotrypsin’s specificity pocket? What would happen if one of those amino acids was changed to lysine? In relation to the amino acid in the specificity pocket, which peptide bond is cleaved; C terminal or N terminal? What is this bond’s proximity to the serine in the active site?
Proteins that span the biological membrane bilayers often contain α-helices and b-barrels. (a) Given that the insides of membranes are highly hydrophobic, predict what type of amino acyl residues would be found in a single alpha-helix that is spanning a membrane – draw a diagram to illustrate the arrangement of the R-groups within the membrane bilayer. (b) Using a drawing, illustrate the R-group arrangement in the membrane-spanning region of a channel protein for water transport if the channel was made of: six alpha-helices six beta-strands
What are the extracellular matrix's effects on secreted proteins? What is the function of a matrix metalloprotease versus a serine protease?
Why would the amount of protein E bound to immobilized heparin fall in the presence of soluble heparin?
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.
In cells, microtubule assembly depends on other proteins as well as tubulin concentration and temperature. What types of proteins influence microtubule assembly in vivo, and how does each type affect assembly?
The nuclear import of proteins larger than 40 kDa requires the presence of what amino acid sequence? Describe the mechanism of nuclear import. How are nuclear transport receptors able to get through the nuclear pore complex?
Draw a fractional binding curve for trimeric protien that has a binding site on each subunit. Moreover, the protein has a preferred low affinity conformation.
Previously Protein A and 5mM of ligand X were combined in a neutral solution and 36% of Protein A was ligand bound. Now Protein A and ligand X are combined in an acidic solution. You now find that when there’s a 4 mM concentration of free ligand X, 45% of the protein is bound to ligand. How does a change in pH affect protein A’s affinity for ligand X? a. Protein A has a higher affinity for ligand X in acidic environments b. Protein A has a lower affinity for ligand X in acidic environments c. The solution pH does not affect the affinity of protein A for ligand X. d. The solution pH does not affect the affinity of a protein for a ligand.

SEE MORE QUESTIONS

Recommended textbooks for you

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

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

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

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

SEE MORE TEXTBOOKS

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.