At high salt concentration, proteins are less soluble. Changing the solubility of a protein based on the concentration of a highly soluble salt is the basis of salt precipitation. Group of answer choices BOTH statements are TRUE. The SECOND statement is TRUE. NONE of the statements are TRUE. The FIRST statement is TRUE.

At high salt concentration, proteins are less soluble. Changing the solubility of a protein based on the concentration of a highly soluble salt is the basis of salt precipitation. Group of answer choices BOTH statements are TRUE. The SECOND statement is TRUE. NONE of the statements are TRUE. The FIRST statement is TRUE.

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

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Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
During the folding of a protein in a buffered aqueous solution, what happens to the entropy of the protein and the entropy of the water? The entropy of the protein decreases while the entropy of the water increases. Both the entropy of the protein and the entropy of the water increase. Both the entropy of the protein and the entropy of the water decrease. The entropy of the protein decreases while the entropy of the water remains constant.
At low salt concentration, proteins are less soluble
Which of the following might cause the denaturation of a protein? Select all that apply. A.)Highly acidic conditions B.)Highly basic conditions C.)High concentrations of salt D.)High heat
Under what pH conditions can a protein not bind to the beads in a column? pH = 7 pH = pI pH = pKa pH = -pKa
Denaturation of protein is a loss of protein structure. Given enough time, can all denatured protein spontaneously renature? Justify answer
Affinity and specificity of protein-protein interactions are mainly mediated by many weak chemical bonds such as: Group of answer choices van der Waals forces hydrogen bonds hydrophobic interactions all of the above
Which of the following is TRUE, if the protein pH is electrically neutral? Refer to the graph below. a. The denaturation of protein is lower than 100% b. The denaturation of protein is greater than 100% c. The protein is in native form d. The protein is completely denatured
which of the following is correct about protein hydration? a- hydrophobic pathces are hydrated first followed by exposed polar side chains. b- the monolayer water that hydreates proteins are those that hydrate ionic, polar, and nonpolar amino acids on the surface of the protein c- polar amino acids are the first hydrated followed by ionic aminio acids d- hydration of hydrophoic patches in proteins is not possible
Which of the following about protein denaturation is not trueA. It is always irreversible B. It is a shape change C. It may be due to pH / temperature change D. Most of the proteins denature when transferred from aqueous environment to organs solvents E. Its function is lost.
At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? Heating a protein (due to fever), causing hydrogen bonds to break. Drastic changes in pH (like the above patients), causing some polar amino acids to turn into non-polar amino acids
Based on the characteristic given, determine which level of protein structure is being referred to. 3D arrangement of localized regions of proteins A. PRIMARY B. SECONDARY