1answer.
Ask question
Login Signup
Ask question
All categories
  • English
  • Mathematics
  • Social Studies
  • Business
  • History
  • Health
  • Geography
  • Biology
  • Physics
  • Chemistry
  • Computers and Technology
  • Arts
  • World Languages
  • Spanish
  • French
  • German
  • Advanced Placement (AP)
  • SAT
  • Medicine
  • Law
  • Engineering
Nat2105 [25]
2 years ago
7

A solution prepared by mixing 10 ml of 1 m hcl and 10 ml of 1.2 m naoh has a ph of

Chemistry
1 answer:
blagie [28]2 years ago
7 0

Answer: pH of resulting solution will be 13

Explanation:

pH is the measure of acidity or alkalinity of a solution.

Moles of H^+ ion = Molarity\times {\text {Volume in L}}=1M\times 0.01L=0.01mol

Moles of OH^- ion = Molarity\times {\text {Volume in L}}=1.2M\times 0.01L=0.012mol

HCl+NaOH\rightarrow NaCl+H_2O

For neutralization:

1 mole of H^+ ion will react with 1 mole of OH^- ion

0.01 mol of H^+  ion will react with =\frac{1}{1}\times 0.01mole of OH^- ion

Thus (0.012-0.01)= 0.002 moles of OH^- are left in 20 ml or 0.02 L of solution.

[OH^-]=\frac{0.002}{0.02L}=0.1M

pOH=-log[OH^-]

pOH=-log[0.1]=1

pH+pOH=14

pH=14-1=13

Thus the pH of resulting solution will be 13

You might be interested in
What is the chemical formula for the ionic compound calcium chloride?
Juliette [100K]

The answer to your question is,

B) CaCl2

-Mabel <3

6 0
3 years ago
Read 2 more answers
In solid NaCl, the equilibrium separation between neighboring Na+ and Cl- ions is 0.283 nm. Calculate the coulombic energy betwe
const2013 [10]

Explanation:

It is given that r = 0.283 nm. As 1 nm = 10^{-9} m.

Hence, 0.283 nm = 0.283 \times 10^{-9} m

  • Formula for coulombic energy is as follows.

             U_{coulomb} = -1.748 \frac{e^{2}}{4 \pi \epsilon_{o} r}

where,   e = 1.6 \times 10^{-19} C

            \epsilon_{o} = 8.85 \times 10^{-12}

          U_{coulomb} = -1.748 \frac{(1.6 \times 10^{-19}^{2}}{4 \times 3.14 \times 8.85 \times 10^{-12} \times 0.283 \times 10^{-9}}

                         = 1.423 \times 10^{-18} J

  • As 1 eV = 1.6 \times 10^{-19} J

So,       1 J = \frac{1 eV}{1.6 \times 10^{-19}}

Hence,    U = \frac{1.423 \times 10^{-18} J}{1.6 \times 10^{-19} J}

                   = 8.9 eV

  • Also,   1 J = \frac{10^{-3} kJ}{6.022 \times 10^{23}mol}

                = 1.67 \times 10^{-27} kJ/mol

Therefore, U = 1.423 \times 10^{-18} J \times 1.67 \times 10^{-27} kJ/mol

                     = 2.37 \times 10^{-45} kJ/mol

7 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
What is the mass of 1 mole of magnesium (Mg)? Express your answer to four significant figures.
Kay [80]

Answer:

24.305 grams

Explanation:

6 0
3 years ago
Read 2 more answers
(ii) Describe another method for making ethanol.​
Aloiza [94]

Answer:

There are essentially three methods used to produce ethanol:

Manufacture from ethene using steam (the "synthetic" route)

Production from sugars and starches by fermentation, using yeasts.

Production from biomass waste, using bacteria.

Please give brainlist if this helped

7 0
2 years ago
Other questions:
  • In order to prepare very dilute solutions, a lab technician chooses to perform a series of dilutions instead of measuring a very
    10·1 answer
  • A 151.5-g sample of a metal at 75.0°C is added to 151.5 g at 15.1°C. The temperature of the water rises to 18.7°C. Calculate the
    12·1 answer
  • What is the number of molecules of c2h5oh in a 3m solution that contains 4.00kg h2o?
    9·1 answer
  • The half-life period for a first order reaction is independent of
    8·2 answers
  • Which is the correct name of this compound CoS
    11·1 answer
  • ENG
    11·1 answer
  • An atom of element Be has four protons, four electrons, and five neutrons. Which element below could be an isotope of this atom?
    13·2 answers
  • Tell me, how the different states of matter are different and the same.
    6·1 answer
  • Convert 9.32x 10 23ª atoms of au to moles of au
    7·1 answer
  • Receiving an electrical shock when you forget to turn off the power before working on an electrical socket is an example of a ne
    8·1 answer
Add answer
Login
Not registered? Fast signup
Signup
Login Signup
Ask question!