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Hatshy [7]
3 years ago
8

Question 2

Chemistry
1 answer:
Mazyrski [523]3 years ago
7 0

There is an increase in the frequency of particle collisions which leads to the increased rate of the reaction.

<u>Explanation:</u>

Hydrochloric acid reacts faster with the powdered zinc than with the equal mass of zinc strips.  

Since the surface area of the Zinc particle increases when it is powdered and has more active spots when compared to less number of active sites in Zinc strips and so the number of collision between the Zinc particles and the particles of Hydrochloric acid also increases and consequently the rate of the reaction also enhances.

So there is an increase in the frequency of particle collisions.

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Which describes why Mendeleev succeeded where others failed?
wolverine [178]

Answer:

  • <em>He realized that some elements had not been discovered.</em>

Explanation:

Some scientists that tried to arrange the list of elements known before Mendeleev include Antoine Lavoisier, Johann Döbereiner, Alexandre Béguyer de Chancourtois, John Newlands, and Julius Lothar Meyer.

<em>Dimitri Mendeleev</em> was so succesful that he is recognized as the most important in such work.

Mendeleev by writing the properties of the elements on cards elaborated by him, and "playing" trying to order them, realized that, some properties regularly (periodically) repeated.

The elements were sorted in increasing atomic weight (which is not the actual order in the periodic table), but when an element did not meet the pattern discovered, he moved it to a position were its properties fitted.

The amazing creativity of Mendeleev led him to leave blanks for what he thought were places that should be occupied by elements yet undiscovered. More amazing is that he was able to predict the properties of some of those elements.

When years after some of the elements were discovered, the genius of Mendeleev was proven because the "new" elements had the properties predicted by him.

7 0
2 years ago
Complete the dissociation reaction and the corresponding Ka equilibrium expression for each of the following acids in water. (Ty
anastassius [24]

Answer :

(A) The dissociation reaction of HC_2H_3O_2 will be:

HC_2H_3O_2(aq)\rightleftharpoons H^+(aq)+C_2H_3O_2^-(aq)

The equilibrium expression :

K_a=\frac{[H^+][C_2H_3O_2^-]}{[HC_2H_3O_2]}

(B) The dissociation reaction of Co(H_2O)_6^{3+} will be:

Co(H_2O)_6^{3+}(aq)\rightleftharpoons H^+(aq)+Co(H_2O)_5(OH)^{2+}(aq)

The equilibrium expression :

K_a=\frac{[H^+][Co(H_2O)_5(OH)^{2+}]}{[Co(H_2O)_6^{3+}]}

(C) The dissociation reaction of CH_3NH_3^+ will be:

CH_3NH_3^+(aq)\rightleftharpoons H^+(aq)+CH_3NH_2(aq)

The equilibrium expression :

K_a=\frac{[H^+][CH_3NH_2]}{[CH_3NH_3^+]}

Explanation :

Equilibrium constant : It is defined as the equilibrium constant. It is defined as the ratio of concentration of products to the concentration of reactants.

The equilibrium expression for the reaction is determined by multiplying the concentrations of products and divided by the concentrations of the reactants and each concentration is raised to the power that is equal to the coefficient in the balanced reaction.

As we know that the concentrations of pure solids and liquids are constant that is they do not change. Thus, they are not included in the equilibrium expression.

(A) The dissociation reaction of HC_2H_3O_2 will be:

HC_2H_3O_2(aq)\rightleftharpoons H^+(aq)+C_2H_3O_2^-(aq)

The equilibrium expression of HC_2H_3O_2 will be:

K_a=\frac{[H^+][C_2H_3O_2^-]}{[HC_2H_3O_2]}

(B) The dissociation reaction of Co(H_2O)_6^{3+} will be:

Co(H_2O)_6^{3+}(aq)\rightleftharpoons H^+(aq)+Co(H_2O)_5(OH)^{2+}(aq)

The equilibrium expression of Co(H_2O)_6^{3+} will be:

K_a=\frac{[H^+][Co(H_2O)_5(OH)^{2+}]}{[Co(H_2O)_6^{3+}]}

(C) The dissociation reaction of CH_3NH_3^+ will be:

CH_3NH_3^+(aq)\rightleftharpoons H^+(aq)+CH_3NH_2(aq)

The equilibrium expression of CH_3NH_3^+ will be:

K_a=\frac{[H^+][CH_3NH_2]}{[CH_3NH_3^+]}

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3 years ago
What is the correct label for a solution?
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The answer is a. a homogenous mixture

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32P can be used to make any nucleotide (A, C, G, or T) radioactive. Which of the following explains why this is true?
xxMikexx [17]
B. The answer is: All nucleotides have a phosphorus atom that can be replaced with 32P.

Nucleotides contain a nitrogenous base, a five-carbon sugar, and, at least, one phosphate group. Exactly that phosphate group in the nucleotide has the phosphorus atom. Therefore, the phosphorus atom in the nucleotide can be replaced with radioactive phosphorus-32 (32P). 
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2 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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