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KiRa [710]
3 years ago
14

Water is placed outside at 298 K overnight. Which statement best describes what would happen?a)298 K converts to -24.9 °C, so th

e water would freezeb)298 K converts to 24.9 °C, so the water would remain in its liquid statec)298 K converts to 24.9 °C, so the water would freeze
Chemistry
1 answer:
user100 [1]3 years ago
7 0

Answer: b)298 K converts to 24.9 °C, so the water would remain in its liquid state

Explanation: Kelvin is an absolute temperature scale, that means that 0K (zero Kelvin) is the lowest temperature possible and compare to Celsius scale the change of 1 degree is the same, but 0°C is the same as 273,1K

So, in order to convert Kelvin to Celsius you have to subtract 273,1

In this case, 298K - 273,1 = 24,9°C

This temperature is room temperature, so water is in liquid state.

You might be interested in
A. what is atmospheric pressure?
Vanyuwa [196]

Answer:

<em>What is atmospheric pressure? -------> Atmospheric pressure is a force in an area pushed against a surface by the weight of the atmosphere of Earth, a layer of air.</em>

<em>Why does the atmosphere exert pressure? -------> Because gas particles in the air—like particles of all fluids—are constantly moving and bumping into things, so they exert pressure. </em>

<em>What is the value of atmospheric pressure at sea level, in newtons per square centimeter? -------> Atmospheric pressure at sea level is about 10 N/cm2 or 100 kPa or about 10 m of water or about 760 mm of mercury, but varies with the weather, and of course altitude.</em>

<em>I hope this helps and have a great day!</em>

Explanation:

6 0
2 years ago
Please refer to image please
GarryVolchara [31]

Answer:

76.9L

Explanation:

Based on the graph, whenever the temperature increases by 100K, the volume increases by 10L, so do 769/10

7 0
2 years ago
The aldol reaction is catalyzed by acid as well as base. What is the reactive nucleophile in the acid-catalyzed aldol reaction
svp [43]

Answer:

The reactive nucleophile is Ketone.

Explanation:

In organic chemistry, The process of acid - catalyzed aldol condensation starts from when ketone (or any aldehyde) is converted to an -enol, after which it attacks another ketone/aldehyde that has already been activated by parbonyl oxygen protonation.

The process of this is that first of all the ketone undergoes tautomerization to form -enol. Thereafter, the other carbonyl will undergo protonation which makes the carbon activated towards attack. Now, the nucleophilic enol will be added to the carbonyl in a [1,2]-addition reaction and we will now use deprotonation to obtain the neutral Aldol product.

Now, since only the ketone can produce an -enol, thus it is the nucleophile as aldehydes are better electrophiles

4 0
3 years ago
Assume the molality of isoborneol in your product is 0.275 mol/kg. What is the melting point of your impure sample given that th
aliina [53]

Answer:

168°C is the melting point of your impure sample.

Explanation:

Melting point of pure camphor= T =179°C

Melting point of sample = T_f = ?

Depression in freezing point = \Delta T_f

Depression in freezing point  is also given by formula:

\Delta T_f=i\times K_f\times m

K_f = The freezing point depression constant

m = molality of the sample  = 0.275 mol/kg

i = van't Hoff factor

We have: K_f = 40°C kg/mol

i = 1 (  non electrolyte)

\Delta T_f=1\times 40^oC kg/mol\times 0.275 mol/kg

\Delta T_f=11^oC

\Delta T_f=T- T_f

T_f=T- \Delta T_f=179^oC-11^oC=168^oC

168°C is the melting point of your impure sample.

4 0
3 years ago
irvinase is an enzyme that has 4 cys residues tied up in 2 disulfide bonds. you denature irvinase with 8m urea in the presence o
Elena L [17]

Answer:

1. Quaternary structure of proteins relates to the interactions between separate polypeptide chains within the protein. The word polypeptide refers to a polymer of amino acids. A protein may contain one or more polypeptides and is folded and may be covalently modified.

2. Hemoglobin (and many other proteins) have multiple polypeptide subunits. Interactions between the subunits include ionic interactions, hydrogen bonds, and hydrophobic interactions. Modification of the quaternary structure of a protein may have the same effects as modification of its tertiary structure - alteration of its function/activity.

3. The enzyme ribonuclease (RNase) is interesting in being very stable to heat and other things that denature/inactivate other proteins. (By the way, denaturation is a word that means the tertiary and/or quaternary structure of a protein is disrupted.). RNase has disulfide bonds that help it to remain resistant to denaturation. Heating it to 100 Celsius, which denatures most proteins does not denature RNase. Breaking the disulfide bonds of RNAse with a reagent like mercaptoethanol followed by heating to 100 Celsius to destroy hydrogen bonds (or treatment with urea) causes loss of activity. If one allows the hydrogen bonds to reform slowly, some of the enzyme's activity reappears, which indicates that the information necessary for proper folding is contained in the primary structure (amino acid sequence).

4. Disulfide bonds are important structural components of proteins. They form when the sulfhydryls of two cysteines are brought together in close proximity. Some chemicals, such as mercaptoethanol, can reduce the disulfides (between cysteine residues) in proteins to sulfhydryls. In the process of transferring electrons to the cysteines, the sulfhydryls of mercaptoethanol become converted to disulfides. Treatment of RNase with mercaptoethanol reduces RNAse's disulfides to sulfhydryls. Subsequent treatment of RNase with urea disrupts hydrogen bonds and allows the protein to be denatured.

5. Interestingly, removal of the mercaptoethanol and urea from the solution allows RNase to refold, reestablish the correct disulfide bonds, and regain activity. Clearly, the primary sequence of this protein is sufficient for it to be able to refold itself to the proper configuration.

6. Other forces besides disulfide bonds that help to stabilize tertiary structure of proteins include hydrogen bonds, metallic bonds, ionic bonds, and hydrophobic bonds.

7. Chemicals that can disrupt some of these forces include urea or guanidinium chloride (disrupts hydrogen bonds), protons (ionic bonds), and detergents (hydrophobic bonds). In addition, dithiothreitol (DTT) can break disulfide bonds and make sulfhydryls.

8. Proteins sometimes have amino acids in them that are chemically modified. Chemical modification of amino acids in proteins almost always occurs AFTER the protein is synthesized (also described as post-translational modification). Examples include hydroxyproline and hydroxylysine in collagen, gamma carboxyglutamate, and phosphoserine. Modification of the collagen residues allows for the triple helical structure of the protein and for the strands to be cross-linked (an important structural consideration).

9. Hemoglobin (and many other proteins) have multiple polypeptide subunits. Interactions between the subunits include disulfide bonds, ionic interactions, hydrogen bonds, hydrophilic, and hydrophobic interactions. Modification of the quaternary structure of a protein may have the same effects as modification of its tertiary structure - alteration of its function/activity.

10. Folding is necessary for proteins to assume their proper shape and function. The instructions for folding are all contained in the sequence of amino acids, but we do not yet understand how those instructions are carried out rapidly and efficiently. Levinthal's paradox illustrates the fact that folding is not a random event, but rather based on an ordered sequence of events arising from the chemistry of each group.

11. Proper folding of a protein is essential. Cells have complexes called Chaperonins that help some proteins to fold properly. Misfolding of proteins is implicated in diseases such as mad cow disease and Creutzfeld-Jacob disease in humans. The causative agent in these diseases is a "contagious" protein that is coded by the genome of each organism. When it doesn't fold properly, it helps induce other copies of the same protein to misfold as well, resulting in plaque-like structures that destroy nerve cells.

Explanation:

8 0
3 years ago
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