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aalyn [17]
3 years ago
11

The water molecule H2O is polar because it contains two polar single bonds and A. its molecule has a linear shape. B. molecules

that contain polar bonds are always polar. C. its molecule has a bent shape. D. the attractions between water molecules are strong. 
Chemistry
2 answers:
Musya8 [376]3 years ago
8 0

Answer: Option (C) is the correct answer.

Explanation:

Water is a polar molecule because it has two polar single bonds and also it has bent shape structure.

Since the oxygen atom of water has two lone pair of electrons and also dipole moment is more towards the oxygen atom. As a result, there will be increase in electron density across the oxygen atom which will induce a negative charge on oxygen and positive charge on hydrogen atom.

Thus, water molecule becomes polar in nature.

Anni [7]3 years ago
4 0
<span>c. it has a bent shape</span>
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8 0
3 years ago
Determine the freezing point and boiling point of a solution that has 68.4 g of sucrose
Ymorist [56]

Answer:

Freezing T° of solution = - 3.72°C

Boiling T° of solution =  101.02°C

Explanation:

To solve this we apply colligative properties. Firstly, freezing point depression:

ΔT = Kf . m . i

ΔT = Freezing T° of pure solvent - Freezing T° of solution

Kf = Cryoscopic constant, for water is 1.86 °C/m

m = molality (moles of solute in 1kg of solvent)

i = Ions dissolved in solution

Our solute is sucrose, an organic compound so no ions are defined. i = 1.

Let's determine the moles: 68.4 g . 1mol/ 342g = 0.2 moles

molality = 0.2 mol / 0.1kg of water = 2 m

We replace data: ΔT = 1.86°C/m . 2m . 1

Freezing T° of solution = - 3.72°C

Now, we apply elevation of boiling point: ΔT = Kb . m . i

ΔT = Boiling T° of solution - Boiling T° of  pure solvent

Kf = Ebulloscopic constant, for water is 0.512 °C/m

We replace:

Boiling T° of solution - Boiling T° of pure solvent = 0.512 °C/m . 2 . 1

Boiling T° of solution = 0.512 °C/m . 2 . 1 + 100°C → 101.02°C

6 0
2 years ago
A shiny, smooth piece of black plastic and an identical piece of white plastic are exposed to visible light and sound waves. Whi
Nana76 [90]

Answer:

The awnser is D

Explanation:

Since the black pieces absorb light better than white pieces, the white pieces will reflect light better. But since color doesn't affect sound, the sound waves are reflected the same.

7 0
2 years ago
Which of the following groups have seven valence electrons and are very reactive?
valina [46]

Answer:

Column 17 halogens

Explanation:

To answer the question we need to know the following;

What are valence electrons?

  • Valence electrons are outermost electrons in the outermost energy level of an atom of any element.

What are halogens?

  • Halogens are group 7 elements that have seven valence electrons. They include, chlorine, fluorine, iodine, etc

What is the reactivity of halogens?

  • Halogens are the most reactive non-metals in the periodic table. They react by gaining one electron to attain a stable configuration.
4 0
3 years ago
Read 2 more answers
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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