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sergejj [24]
1 year ago
13

Project 1 Hypothesis Construction

Chemistry
1 answer:
alukav5142 [94]1 year ago
5 0

The hypothesis should be; "Increasing the amount of ice increases the rate at which the ice will melt"

<h3>What is a hypothesis?</h3>

The term hypothesis refers to a tentative explanation that could be applied in order to explain an observation. When we give a hypothesis, it must be subjected to rigorous experimentation thus it can be confirmed or repelled by experiment.

Now, we can see that the question here is; "How does the amount of salt added to ice affect the rate at which the ice will melt?" This implies that the correct hypothesis here ought to have to do with the impact of the amount of ice in the affirmative.

Thus, the hypothesis should be; "Increasing the amount of ice increases the rate at which the ice will melt"

Learn more about hypothesis:brainly.com/question/13025783

#SPJ1

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One compound that contributes to the "seashore smell" at beaches in Hawaii is dictyopterene D', a component of a brown edible se
Luba_88 [7]

Answer:

Explanation:

There are few simple rules in organic chemistry which a person must learn.

1. In predicting a structure from ozonolysis, number of oxygen present in products must be counted. In this particular example, there are 2+3+1 = 6 oxygen atoms are present in three molecules. This means that there should be at least three confirmed double bonds must be present in the molecule of Dictyopterene.

2. There are in total of 3+5+3 = 11 carbon atoms present, making 2^11 = 2048 possible structures for this particular structure. But since there are three double bonds present, this will reduce the number of possible structures as well.

3. Questions also says that when fully hydrogenated, the molecule generates Butylcycloheptane. That means that our base molecule is Butylcycloheptane and this molecule contains at least three double bonds.

So, first we draw the molecule of butylcycloheptane. After this, we think of were double bonds could be present. We do have the products. Let's make their structures first. I have also mentioned the possible breakup where the ozonolysis has occured by color code. You can see them in the reference image attached.

Part 1 out of 2: There is only one chiral carbon present in the molecule and have two possible isomers. Cis and Trans. Only one stereogenic carbon is present, that's why two possible isomers. Image attached.

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
Type your answer in decimal form. Do not round.<br> 7 days = hours
djyliett [7]
168.0
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5 0
2 years ago
Read 2 more answers
Can you identify a chemical only by knowing its physical properties?
amid [387]

Answer:

Any characteristic that can be determined without changing the substance's chemical identity. chemical property: Any characteristic that can be determined only by changing a substance's molecular structure

Explanation:

4 0
2 years ago
ILL GIVE BRAINLIEST IF CORRECT!!! students who enjoy acting out plays likely think with what part of their brains?
tresset_1 [31]

Answer:

B

Explanation:

The front brain(cerebrum) is the part of the brain that controls important cognitive skills in humans, such as emotional expression, problem solving, memory, language, judgment, and sexual behaviors.

Here the students who enjoy acting out plays likely think with front brain. I guess so..

6 0
3 years ago
Read 2 more answers
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