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Chemistry Assignment

Short Answer Questions:

Hormone signaling in the human body

Cells react to a hormone when they express a particular receptor for that hormone. The
hormone ties to the receptor protein, bringing about the initiation of a sign transduction
mechanism that at last prompts cell-type-specific reactions. The binding of receptors tends
to alter the activity of the cells which results in an increase or decrease in the body
processes. Depending on where the protein receptor is located on the target cell and how
the hormone is chemically structured, hormones intervene changes in either of the two
ways; directly binding to the intracellular hormone receptors which modulate gene
transcription, or indirectly binding to the surface to the cell receptors which stimulates
signaling pathways.

Effects of molecules on tissues of the body

Testosterone, estradiol, and cortisol are similar in structures but have different effects on
the tissues of the body. Testosterone is a male sex hormone that stimulates the formation
of sperms, provides secondary sexual characteristics, and promotes and develops the male
duct system in the fetus. Estradiol, secreted in the females, is responsible for several female
sex characteristics. Cortisol, on the other hand, is secreted by the cortex and is a
glucocorticoid, helps in raising blood-glucose levels by breaking down proteins and fats.
It also suppresses the immune and inflammatory response.

Effectiveness of detergents in lysing cell membrane

Surfactants, which commonly called as detergents, have the characteristic of disrupting the
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interface between hydrophobic and hydrophilic systems. Biological membranes, that have
hydrophobic/hydrophilic interfaces, are the initial targets of detergents. For example, in E.
coli and SDS, the detergent effectively and completely obliterates the distinct interface by
separating the cell from its environment, which is, the membrane. Detergents have a cone-
shaped structure, while phospholipids are cylindrical.

Presence of amino acids of side chains

The active sites are catalytic since the amino acids contained in them take part in the
chemical reaction which is catalyzed by an enzyme. The active and catalytic site of the
enzymes is a steric and unusual electrostatic environment wherein both reactants and side
chains are clubbed together in a mixture. The crowding of side chains and reactants is
essential for the catalytic function. The activity of the enzyme id based on the structure of
its active site. This is important for the binding of the substrate and the occurrence of
reaction between side chains and substrate. All this depends on the structure of the protein.
If the structure of the enzyme is affected, its capacity of catalysis gets affected.

Insertion and deletion mutations

DNA can be changed in different ways which result in different kinds of mutations. Insertion
mutations are the ones in which extra base pairs are inserted into a new place in the DNA.
Deletion mutations are the ones in which an entire section of DNA is deleted or lost. These
mutations are serious than substitution mutations because, in substitution mutations, only a
codon is changed or replaced. Whereas in these, either extra base pairs are added, or a
section od DNA is completely deleted. This affects the functionality of the DNA much higher.

Amylose and cellulose

Differences:
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• Amylose has α-1,4-glycosidic bonds, while cellulose has β (1→4) glycosidic bonds.

• Humans can process amylose however not cellulose.

• Glucose particles in cellulose are found in an alternative form where one is down

and one is up, yet in amylose, glucose molecules are in a similar direction.

• Amylose is in starch, and they fill in as the energy storage compound in plants.

Cellulose is essentially a basic compound, which takes an interest in cell wall

development in plants.

Similarities:

• Both amylose and cellulose are polysaccharides.

• Both contain glycosidic bonds in condensation reactions.

• Both are not soluble in water

• Both contain unbranched chains

Amylase is responsible for breaking the bonds in amylose. However, it can’t break the bonds
in cellulose. The active site in amylase helps in breaking down the bonds between uniform
and straight chains in cellulose. In cellulose, the bonds between the glucose molecules exist
in an entirely different shape and hence require an active site that is shaped differently
completely to break them down.
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Essay Questions:
Carbohydrates:

Saltine cracker molecules

The process of digestion includes breaking down of food into several nutrients which the
body can use. When saltine crackers are first put into the mouth the teeth chew them into
smaller pieces. This is called physical digestion. The crackers in the mouth get mixed with
saliva. Saliva contains enzymes and chemicals which break down the food particles into
simpler pieces. The stomach and small intestine break these food particles into even smaller
pieces. When chemicals and enzymes break down food, the process is called chemical
digestion.

Saliva contains an enzyme called amylase which breaks down the starch and complex
carbohydrates present in the saltine crackers into simple sugars like maltose and dextrin.
The body cannot use larger molecules of starch, so enzymes break these molecules into
smaller sugar molecules which get absorbed by the body and can be used later.

Glucagon is secreted from the pancreatic alpha cells in the islet of Langerhans. It plays an
essential role in glucose homeostasis when it stimulates hepatic glucose production.
Glucagon is a glucose mobilizing hormone.

Deficiency in glucagon leads to many diseases:

Diseases related to unnecessarily high or low discharge of glucagon are uncommon.

Malignant growths of alpha cells (glucagonomas) are one circumstance known to cause over
the top glucagon emission. These tumors ordinarily lead to wasting syndrome and, rash, and
other skin injuries.
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Even though insulin insufficiency is the significant deformity in type 1 diabetes mellitus,
there is extensive proof that deviant discharge of glucagon adds to the metabolic
disturbances found in this significant disease. For instance, numerous diabetic patients with
hyperglycemia likewise have raised blood convergences of glucagon, yet glucagon emission
is ordinarily smothered by raised degrees of blood glucose.

Proteins:

Denaturation is a process in which the structure of proteins gets disrupted due to external
factors. This happens due to the disruption of the weaker chemical interactions and bonds
which later become biologically inactive.

a. Denaturation by heat

Most proteins can be denatured through heat. This affects the weaker interactions in the
proteins, which are hydrogen bonds primarily, and happens in a complex manner. If the
temperature is slowly increased the confirmation of the protein remains intact generally.
However, if the temperature range is narrow, the protein loses its structure and function
abruptly.

b. Denaturation by strong acids

Strong acids disrupt the salt bridges in proteins which are held by ionic bonds. Occurrence of
double replacement reaction happens when the positive and negative ions change their
partners with the positive and negative ions of the acid added.

c. Denaturation reducing agents

Reducing agents disrupt the structure of the proteins by breaking the disulfide bonds.
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Disulfide bonds are framed by oxidation of sulfhydryl bunches on cysteine. Diverse protein
chains or circles inside a solitary chain are held together by the solid covalent disulfide
bonds. Since oxidizing agents lead to the formation of disulfide bonds, reducing agents
would act to split them up.

Transcription and translation:

Sickle cell anemia

Sickle cell disease is a group of disorders that influences hemoglobin, the atom in red
platelets that conveys oxygen to cells all through the body. Individuals with this issue have
atypical hemoglobin atoms called hemoglobin S, which can mutilate red platelets into a
sickle, or bow, shape.

Any kind of mutation in the HBB gene would cause sickle cell disease.

Hemoglobin comprises of four protein subunits, ordinarily, two subunits called alpha-globin
and two subunits called beta-globin. The HBB quality gives guidelines for making beta-
globin. Different forms of beta-globin result from various transformations in the HBB
quality. One specific HBB quality change creates a strange variant of beta-globin known as
hemoglobin S (HbS). Different changes in the HBB quality lead to extra irregular forms of
beta-globin, for example, hemoglobin C (HbC) and hemoglobin E (HbE). HBB quality changes
can likewise bring about a strangely low degree of beta-globin; this variation from the norm
is called beta-thalassemia.

In individuals with sickle cell disease, in any event one of the beta-globin subunits in
hemoglobin is supplanted with hemoglobin S. In sickle cell anemia, which is a typical type of
sickle cell disease, hemoglobin S replaces both beta-globin subunits in hemoglobin. In
different kinds of sickle cell sickness, only one beta-globin subunit in hemoglobin is
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supplanted with hemoglobin S. The other beta-globin subunit is supplanted with an

alternate anomalous variation, for example, hemoglobin C. For instance, individuals with
sickle-hemoglobin C (HbSC) ailment have hemoglobin atoms with hemoglobin S and
hemoglobin C rather than beta-globin. On the off chance that changes that produce
hemoglobin S and beta-thalassemia happen together, people have hemoglobin S-beta
thalassemia (HbSBetaThal) illness.

Unusual renditions of beta-globin can mutilate red platelets into a sickle shape. The sickle-
formed red platelets pass on rashly, which can prompt anemia. Many times the resolute,
sickle-formed cells stall out in little veins and can cause genuine clinical complications.

Transcription and translation in protein synthesis

Cell utilizes the qualities to combine proteins. This is a two-advance procedure. The initial
step is a transcription in which the sequence of one quality is repeated in an RNA particle.
The subsequent advance is the translation in which the RNA atom fills in as a code for the
development of an amino-corrosive chain (a polypeptide).

Transcription

For a gene to be communicated, i.e., converted into RNA, that bit of the DNA must be
uncoiled and liberated of the defensive proteins. A catalyst, called DNA polymerase,
"peruses" the DNA (the sequence of bases on one of the two strands of the DNA particle)
and constructs a solitary abandoned chain of the RNA atom as a correlative, identical
representation sequence. Once more, where there is a G in DNA, there will be C in the RNA
and the other way around. Rather than thymine, RNA has uracil(U). Any place in the DNA
strand there is an A, there will be a U in the RNA, and any place there is a T on the DNA
atom, there will be An in the RNA.
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When the entire quality (100s to 10,000s of bases straight) is deciphered, the RNA atom
confines. The RNA (called detachment RNA or mRNA) might be additionally adjusted by the
option of increasingly A bases at its tail, by the option of other little particles to a portion of
the nucleotides and by extraction of certain bits (introns) out of the chain. The evacuation of
introns (the non-coding districts) and assembling the rest of the portions - exons - into a
solitary chain once more, is called RNA grafting. RNA joining takes into consideration one
quality to code for numerous related sorts of proteins, as elective examples of grafting
might be constrained by different factors in the cell.

In contrast to DNA, the mRNA particle is equipped for leaving the core through the pores in
the atomic film. It enters the endoplasmic reticulum and joins itself to one of the layers in
the unpleasant ER.

Translation

Three sorts of RNA are associated with the translation procedure: mRNA which conveys the
genetic code, rRNA which helps in the development of the ribosome, and tRNA which
carries singular amino-acids to the ribosome. Translation is constrained by different
catalysts that perceive explicit nucleotide sequences.

The genetic sequence (nucleotide sequence of a quality) converts into a polypeptide

(amino-corrosive sequence of a protein) in a 3-to-1 design. Three nucleotides straight code
for one amino-corrosive. There are an aggregate of 20 amino-acids used to construct all
proteins in our bodies. Some amino acids are coded by a solitary triplet code, or codon.
Other amino-acids might be coded by a few distinctive RNA sequences. There is likewise a
START sequence (coding for fMet) and a STOP sequence that doesn't code for any amino-
corrosive. The genetic code is (nearly) widespread. Aside from a couple of microorganisms,
all of life utilizes the equivalent genetic code - similar triplets of nucleotides code for a
similar amino-acids.
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At the point when the ribosome is gathered around an atom of mRNA, the translation starts
with the perusing of the principal triplet. Little tRNA particles get the individual amino-acids
and join them to the mRNA, just as to one another, shaping a chain of amino acids. At the
point when a stop signal is reached, the whole perplexing disassociates. The ribosome, the
mRNA, the tRNAs, and the compounds are then either debased or re-utilized for another
translational occasion.

Metabolism

The electron transport chain is a progression of proteins and natural particles found in the
inward layer of the mitochondria. Electrons are passed from one individual from the
transport chain to another in a progression of redox responses. Energy discharged in these
responses is caught as a proton inclination, which is then used to make ATP in a procedure
called chemiosmosis. Together, the electron transport chain and chemiosmosis make up
oxidative phosphorylation.

Electrons delivery by NADH and FADH2

Diminished electron bearers (NADH and FADH2) from different strides of cell respiration
move their electrons to atoms close to the start of the transport chain. All the while, they
turn around into NAD+ and FAD, which can be reused in different strides of cell respiration.

Electron transfer and pumping of proton

As electrons are passed down the chain, they move from a higher to a lower energy level,
discharging energy. A portion of the energy is utilized to pump H+ particles, moving them
out of the framework and into the intermembrane space. This pumping sets up an
electrochemical slope.
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Parting of oxygen molecules to form water

Toward the finish of the electron transport chain, electrons are moved to atomic oxygen,
which parts down the middle and takes up H+ to form water.

Gradient driven synthesis of ATP

As H+ particles stream down their gradient and go into the grid, they go through a catalyst
called ATP synthase, which saddles the progression of protons to synthesize ATP.
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References
[1] Wagner, R., Apriletti, J., McGrath, M. et al. A structural role for hormone in the thyroid
hormone receptor. Nature 378, 690–697 (1995). https://doi.org/10.1038/378690a0

[2] Schneider, W.C. (1946). Intracellular distribution of enzymes; the distribution of succinic
dehydrogenase, cytochrome oxidase, adenosinetriphosphatase, and phosphorus
compounds in normal rat liver and in rat hepatomas. Cancer research, 6 12, 685-90.

[3] Morrisett, J. D., Jackson, R. L., and Gotto, A. M., Jr., Lipoproteins: Structure and
function, Annu. Rev. Biochem. 44:183 (1975).

[4] Simpson, E. R. (2000). Genetic Mutations Resulting in Loss of Aromatase Activity in

Humans and Mice. Journal of the Society for Gynecologic Investigation, 7(1_suppl), S18–
S21. https://doi.org/10.1177/1071557600007001S07

[5] Holden, J. P., Butzow, T. L., Laughlin, G. A., Ho, M., Morales, A. J., & Yen, S. C. (1995).
Regulation of Insulin-Like Growth Factor Binding Protein-I During the 24-Hour Metabolic
Clock and in Response to Hypoinsulinemia Induced by Fasting and Sandostatin in Normal
Women. Journal of the Society for Gynecologic Investigation, 2(1), 38–
44. https://doi.org/10.1177/107155769500200108

[5] Pauling, L., Itano, H., Singer, S., & Wells, I. (1949). Sickle Cell Anemia, a Molecular
Disease. Science, 110(2865), 543-548. Retrieved April 29, 2020, from
www.jstor.org/stable/1676635

[6] Neel, J. (1949). The Inheritance of Sickle Cell Anemia. Science, 110(2846), 64-66.

Retrieved April 29, 2020, from www.jstor.org/stable/1677755

[7] Bonner, J., Huang, R., & Gilden, R. (1963). Chromosomally Directed Protein
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Synthesis. Proceedings of the National Academy of Sciences of the United States of

America, 50(5), 893-900. Retrieved April 29, 2020, from www.jstor.org/stable/71939

[8] Glover, J. (1987). Protein synthesis. The Science Teacher, 54(2), 42-42. Retrieved April 29,
2020, from www.jstor.org/stable/24139610

[9] Ott, T., Clarke, J., Birks, K., & Johnson, G. (1999). Regulation of the photosynthetic
electron transport chain. Planta, 209(2), 250-258. Retrieved April 29, 2020, from
www.jstor.org/stable/23385810