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.

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.

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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Consider a hypothetical amino acid whose side chain forms a hydrogen bond with the oxygen atom of a water molecule. Based on this information, which of the following statements is correct? The side chain of the amino acid is hydrophobic. The side chain of the amino acid is negatively charged. It is not possible to determine if the amino acid is positively charged, negatively charged, or hydrophobic. The side chain of the amino acid is positively charged.
When a protein folds, it forms a more ordered structure. Why does this phenomenon not violate the second law of thermodynamics?
Explain in detail how protein folding is a thermodynamically favored process even though the change in entropy is highly unfavorable.
Despite the thermal stability of covalent bonds in physiological systems, some of these bonds are sensitive to energy input from external sources. The molecule can absorb heat from the environment without changing its chemical structure, as will occur when there is a local temperature increase. If the increase in energy is above kT (i.e., the entire environment has not increased its temperature), the molecule will come to thermal equilibrium with the environment around it, and return to its original energy state. Which one of the following physiological process is example to this? Select one : a. Absorbance of light by 11-cis-retinal. b. Translucent to opaque conversion of egg whites after cooking. C. Absorbance of light by melanın. d. a & b e. a & c f.b&c g. a, b & c
Define entropy and enthalpy. Do living cells increase entropy within themselves? Do they increase entropy in the environment?
Drugs are small molecules that often occur in either a neutral or a charged form, depending on pH. For example, aspirin can be either neutral or lose a proton to be negatively charged. When aspirin is charged, it does not diffuse well into the body. pH varies in the gastrointestinal track. Since the stomach has a low pH (pH=3), it has a larger concentration of neutral aspirin (10-3 M), while the small intestine (pH=6) has a smaller neutral aspirin concentration (10-6 M). For the following, assume that the neutrally charged aspirin molecule has a diffusion coefficient through the cell of 1 x 10-6 cm2/s.
Drugs are small molecules that often occur in either a neutral or a charged form, depending on pH. For example, aspirin can be either neutral or lose a proton to be negatively charged. When aspirin is charged, it does not diffuse well into the body. pH varies in the gastrointestinal track. Since the stomach has a low pH (pH=3), it has a larger concentration of neutral aspirin (10-3 M), while the small intestine (pH=6) has a smaller neutral aspirin concentration (10-6 M). For the following, assume that the neutrally charged aspirin molecule has a diffusion coefficient through the cell of 1 x 10-6 cm2/s. C) We’d like to figure out where in the body aspirin is absorbed as determined by its diffusion rate. If the small intestine has a surface area 50 times that of the stomach, what is the ratio of the diffusion rates in the stomach compared to the small intestine? D) In which part of the GI tract is most of the aspirin absorbed?
Often, complex molecules are described in terms of their atomic masses. But what is more relevant in biology is how they take up space. (For proteins, their shapes are particularly important.) Let's see if we can get an approximate idea of the physical size of a protein molecule by doing various estimations. An important molecule in the internal mechanisms of cells is Actin. This is measured as having a mass of about 42 kDa (= 42,000 Daltons, where 12 Daltons is defined as the mass of a carbon atom). Let's see if we can estimate how big it is using very crude estimates. Of course eventually we will want to know how big it actually is and what its shape is, but getting a scale would help us determine what measurement tools might be appropriate. In order to estimate the size of Actin, we'll first make an estimate of how many atoms it has, then, using the average size of an atom, we'll consider different models of how it might be arranged to get an idea of its size. A. We could look up…
A molecule of glycogen is formed by linking glucose molecules through this process. The separation of polymers into smaller units makes use of this process. This process does not involve breaking peptide bonds, but it does involve unfolding protein structure. The addition of water to break proteins into amino acids is an example of this process. Dehydration Synthesis Using acids to cook raw fish is an example of this process. This process removes water to link two or more amino acids. Denaturation Breaking DNA into nucleotides involves this process. The change to the color and consistency of an egg during cooking is an example of this process. Monomers are linked together through this process. Hydrolysis
Are proteins and enzyme the same in its structure and function. Why? Explain and provide an example in each.
Consider a system consisting of an egg in an incubator. The white and yolk of the egg contain proteins, carbohydrates, and lipids. If fertilized, the egg is transformed from a single cell to a complex organism. Discuss this irreversible process in terms of the entropy changes in the system, surroundings, anduniverse. Be sure that you first clearly define the system and surroundings.
What is the hydrophobic effect, and what drives it: the enthalpy or entropy of the system? (explain your answer)

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		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.