Explain mutarotation of glucose elaborating the

answer with the help of associated structure .

Figure 24.3.124.3.1: Cyclization of D-Glucose. D-Glucose can be represented with a

Fischer projection (a) or three dimensionally (b). By reacting the OH group on the
fifth carbon atom with the aldehyde group, the cyclic monosaccharide (c) is
produced.

When a straight-chain monosaccharide, such as any of the structures shown in

Figure 24.3.124.3.1, forms a cyclic structure, the carbonyl oxygen atom may be
pushed either up or down, giving rise to two stereoisomers, as shown in
Figure 24.3.224.3.2. The structure shown on the left side of Figure 24.3.224.3.2,
with the OH group on the first carbon atom projected downward, represent what is
called the alpha (α) form. The structures on the right side, with the OH group on the
first carbon atom pointed upward, is the beta (β) form. These two stereoisomers of a
cyclic monosaccharide are known as anomers; they differ in structure around
the anomeric carbon—that is, the carbon atom that was the carbonyl carbon atom in
the straight-chain form.

It is possible to obtain a sample of crystalline glucose in which all the molecules have
the α structure or all have the β structure. The α form melts at 146°C and has a
specific rotation of +112°, while the β form melts at 150°C and has a specific rotation
of +18.7°. When the sample is dissolved in water, however, a mixture is soon
produced containing both anomers as well as the straight-chain form, in dynamic
equilibrium (part (a) of Figure 24.3.224.3.2). You can start with a pure crystalline
sample of glucose consisting entirely of either anomer, but as soon as the molecules
dissolve in water, they open to form the carbonyl group and then reclose to form
either the α or the β anomer. The opening and closing repeats continuously in an
ongoing interconversion between anomeric forms and is referred to
as mutarotation (Latin mutare, meaning “to change”). At equilibrium, the mixture
consists of about 36% α-D-glucose, 64% β-D-glucose, and less than 0.02% of the
open-chain aldehyde form. The observed rotation of this solution is +52.7°.

Figure 24.3.224.3.2: Monosaccharides. In an aqueous solution, monosaccharides

exist as an equilibrium mixture of three forms. The interconversion between the
forms is known as mutarotation, which is shown for D-glucose (a) and D-fructose (b).

 Alpha and beta configurations of glucose can change spontaneously through

intermediate open chain formation (the process of Mutarotation). Specific rotation of
alpha form is +1120, specific rotation of beta form is +190. There is gardual change in
optical rotation of the solution. The initial optical rotation changes to a constant optical
rotation (+52.50). The constant specific rotation is due to resultant net optical activity of
both alpha and beta anomers.
The difference between essential and non essential amino acids:

1. Nonessential amino acids can be made by the body, while essential amino

acids cannot be made by the body so you must get them from your diet. You must have all of
the amino acids so your body can build the wide variety of proteins it needs. Protein is
needed for the repair, growth and maintenance of the cells.
2. There are 11 nonessential amino acids: They are arginine, glutamine, tyrosine,
cysteine, glycine, proline, serine, ornithine, alanine, asparagine, and aspartate.
3. Nine out of the 20 amino acids are essential, but adults only need to obtain eight of
them: valine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine and
tryptophan. The ninth amino acid -- histidine -- is only essential for infants.

Draw the structure of Sucrose mentioning the

monomers and the linkage formed

(Source: Wikipedia)

This is the most important disaccharide. It is popularly known

as table sugar. Sucrose is found in all photosynthetic plants. It
is commercially obtained from sugarcane and sugar beets via
an industrial process. Let us take a look at
some chemical properties of sucrose

 The molecular formula of sucrose is C12H22O11.

 If sucrose goes through acid catalysed hydrolysis it will
give one mole of D-Glucose and one mole of D-Fructose.
 The chemical structure of sucrose comprises of α form of
glucose and β form of fructose
 The glycosidic linkage is α linkage because the molecule
formation is in α orientation
  Sucrose is a non-reducing sugar. As you can see from the
structure it is combined (linked) at the
hemiacetal oxygen and does not have a free hemiacetal
hydroxide
 Since has no free hemiacetal hydroxide it does not show
mutarotation (α to β conversion). Sucrose also does not form
osazones for the same reason.
 We can prove the structural formula of sucrose by
hydrolysing it with α-glycosidase enzymes which only
hydrolyses α glucose. This test is positive for sucrose.

Why sucrose known as invert sugar?

When sucrose is hydrolyzed it forms a 1:1 mixture of glucose and fructose.
This mixture is the main ingredient in honey. It is called invert sugar
because the angle of the specific rotation of the plain polarized light
changes from a positive to a negative value due to the presence of the
optical isomers of the mixture of glucose and fructose sugars.

In the hydrolysis of any di- or poly saccharide, a water molecule helps to

break the acetal bond as shown in red. The acetal bond is broken, the H
from the water is added to the oxygen on the glucose.

The -OH is then added to the carbon on the fructose.

To analyze the effect of substrate concentration on the

activity of enzymes.
Enzymes are protein molecules that act as biological catalysts by increasing the rate of reactions without
changing the overall process. They are long chain amino acids bound together by peptide bonds. Enzymes are
seen in all living cells and controlling the metabolic processes in which they converted nutrients into energy and
new cells. Enzymes also help in the breakdown of food materials into its simplest form. The reactants of enzyme
catalyzed reactions are termed as substrates. Each enzyme is quite specific in character, acting on a particular
substrates to produce a particular products. The central approach for studying the mechanism of an enzyme-
catalyzed reaction is to determine the rate of the reaction and its changes in response with the changes in
parameters such as substrate concentration, enzyme concentration, pH, temperature etc .This is known as
enzyme kinetics. 
 
One of the important parameters affecting the rate of a reaction catalyzed by an enzyme is the substrate
concentration, [S]. During enzyme substrate reaction, the initial velocity V0 gradually increases with increasing
concentration of the substrate. Finally a point is reached, beyond which the increase in V 0 will not depend on the
[S]. When we plot a graph with substrate concentration on the X axis and corresponding velocity on Y axis. It can
be observed from the graph that as the concentration of the substrate increases, there is a corresponding
increase in the V0. However beyond  a particular substrate concentration, the velocity remains constant without
any further increase. This maximum velocity of an enzyme catalysed reaction under substrate saturation is called
the Vmax , Maximum velocity.  

                                         

Michaelis – Menten Equation

 
Leonor Michaelis and Maud Menten postulated that the enzyme first combines reversibly with its substrate to
form an enzyme-substrate complex in a relatively fast reversible step:

                                               

                       Eqn.1
In the next step, this ES complex is breaks down in to the free enzyme and the reaction product P:
                                                                               Eqn.2
Since the second step is the rate limiting step, the rate of overall reaction must be proportional to the
concentration of the ES that reacts in the second step. The relationship between substrate concentration, [S] and
Initial velocity of enzyme, V0 (Fig. 1) has the same general shape for most enzymes (it approaches a rectangular
hyperbola). This can be expressed algebraically by the Michaelis-Menten equation. Based on their basic
hypothesis that the rate limiting step in enzymatic reactions is the breakdown of the ES complex to free enzyme
and product, Michaelis and Menten derived an equation which is;
 

                                                                               Eqn.3  

The necessary terms in this reaction are [S], V0, Vmax, and Km (Michaelis constant),. All these terms can be  
measured experimentally.

Importance of Km
Km is the Michaelis-Menten constant which shows the concentration of the substrate when
the reaction velocity is equal to one half of the maximal velocity for the reaction. It can also
be thought of as a measure of how well a substrate complexes with a given enzyme,
otherwise known as its binding affinity.

How does enzyme enhance the rate of a chemical

reaction?

Enzymes are biological catalysts. Catalysts lower the activation energy for
reactions. The lower the activation energy for a reaction, the faster the rate.
Thus enzymes speed up reactions by lowering activation energy. Many
enzymes change shape when substrates bind. This is termed "induced fit",
meaning that the precise orientation of the enzyme required for catalytic
activity can be induced by the binding of the substrate.

Enzymes have active sites. The enzyme active site is the location on the
enzyme surface where substrates bind, and where the chemical reaction
catalyzed by the enzyme occurs. There is a precise substrate interaction
that occurs at the active site stabilized by numerous weak interactions
(hydrogen bonds, electrostatic interactions, hydrophobic contacts, and van
der Waals forces).

Enzymes form complexes with their substrates. The binding of a substrate

to an enzyme active site is termed the "enzyme-substrate complex." A
generic equation for complex formation is as follows:

Enzymes do not:
Change the equilibrium constant for a reaction. Keq depends only on
the difference in energy level between reactants and products.

Change ΔG for a reaction. As shown in the graphs above, enzymes

only lower activation energy, but do not change the difference in
energy levels between reactants and products.
 Nucleotides are building blocks of nucleic acids (DNA and RNA). A nucleic acid
contains a chain of nucleotides linked together with covalent bonds to form a
sugar-phosphate backbone with protruding nitrogenous bases. For example,
DNA contains two such chains spiraling round each other in the famous double
helix shape. The two chains in the double helix are held together along their
length by hydrogen bonds that form between the bases on one chain and the
bases on the other.
The biological functions of nucleotides are:

 Data storage - as part of DNA/RNA

 Energy Currency - ATP
 Cellular communication (cAMP; ATP allosteric regulator)
 Co-enzyme catalysis
 When nucleosides are phosphorylated by specific kinases (a type
of enzyme in the cell on the sugar's primary alcohol group (-CH2-OH),
nucleotides are produced.
 Nucleotidases are hydrolytic enzymes which break down nucleotides
(such as the thymine nucleotide) into nucleosides (such as thymidine)
and phosphate.

Denaturation of Proteins
Denaturation is a process in which proteins or nucleic
acids lose the quaternary structure, tertiary structure,
and secondary structure which is present in their native
state, by application of some external stress or
compound such as a strong acid or base, a
concentrated inorganic salt, an organic solvent
(e.g., alcohol or chloroform), radiation or heat.[3] If
proteins in a living cell are denatured, this results in
disruption of cell activity and possibly cell death. Protein
denaturation is also a consequence of cell death.[4]
[5]
 Denatured proteins can exhibit a wide range of
characteristics, from conformational change and loss of
solubility to aggregation due to the exposure
of hydrophobic groups. Denatured proteins lose their 3D
structure and therefore cannot function.
 Main Differences Between DNA and RNA
Comparison DNA RNA
Name DeoxyriboNucleic Acid RiboNucleic Acid
Function Long-term storage of genetic Used to transfer the genetic code
information; transmission of from the nucleus to the ribosomes
genetic information to make to make proteins. RNA is used to
other cells and new organisms. transmit genetic information in
some organisms and may have
been the molecule used to store
genetic blueprints in primitive
organisms.

Structural B-form double helix. DNA is a A-form helix. RNA usually is a

Features double-stranded molecule single-strand helix consisting of
consisting of a long chain of shorter chains of nucleotides.
nucleotides.

Composition deoxyribose sugar ribose sugar

of Bases and phosphate backbone phosphate backbone
Sugars adenine, guanine, cytosine, adenine, guanine, cytosine, uracil
thymine bases bases

Propagation DNA is self-replicating. RNA is synthesized from DNA on

Base Pairing AT (adenine-thymine)
GC (guanine-cytosine)
Reactivity The C-H bonds in DNA make it
fairly stable, plus the body
destroys enzymes that would
attack DNA. The small grooves
in the helix also serve as
protection, providing minimal
space for enzymes to attach.
an as-needed basis.
AU (adenine-uracil)
GC (guanine-cytosine)
The O-H bond in the ribose of
RNA makes the molecule more
reactive, compared with DNA.
RNA is not stable under alkaline
conditions, plus the large grooves
in the molecule make it
susceptible to enzyme attack.
RNA is constantly produced,
used, degraded, and recycled.

Ultraviolet DNA is susceptible to UV Compared with DNA, RNA is

Damage damage. relatively resistant to UV damage.
 With the help of a graph explain how a competitive
inhibitor changes the Km and Vmax of an
enzyme?

Enzyme kinetics graph showing rate of reaction as a function of

substrate concentration for normal enzyme, enzyme with a
competitive inhibitor, and enzyme with a noncompetitive inhibitor.
For the competitive inhibitor, Vmax is the same as for the normal
enzyme, but Km is larger. For the noncompetitive inhibitor, Vmax is
lower than for the normal enzyme, but Km is the same.

 With a competitive inhibitor, the reaction can eventually reach

its normal V_{max}VmaxV, start subscript, m, a, x, end subscript, but
it takes a higher concentration of substrate to get it there. In other
words, V_{max}VmaxV, start subscript, m, a, x, end subscript is
unchanged, but the apparent K_mKmK, start subscript, m, end
subscript is higher. Why must more substrate be added in order to
reach V_{max}VmaxV, start subscript, m, a, x, end subscript? The
 extra substrate makes the substrate molecules abundant enough to
consistently “beat” the inhibitor molecules to the enzyme.

 With a noncompetitive inhibitor, the reaction can never reach

its normal V_{max}VmaxV, start subscript, m, a, x, end subscript,
regardless of how much substrate we add. A subset of the enzyme
molecules will always be “poisoned” by the inhibitor, so the effective
concentration of enzyme (which determines V_{max}VmaxV, start
subscript, m, a, x, end subscript) is reduced. However, the reaction
reaches half of its new V_{max}VmaxV, start subscript, m, a, x, end
subscript at the same substrate concentration, so K_mKmK, start
subscript, m, end subscript is unchanged. The unchanged K_mKm
K, start subscript, m, end subscript reflects that the inhibitor doesn't
affect binding of enzyme to substrate, just lowers the concentration
of usable enzyme.

Differentiate between psychrophiles and thermophile

Psychrophiles or cryophiles are organisms that are capable of growth

and reproduction in low temperatures, ranging from −20 °C to +10 °C.
They are found in places that are permanently cold, such as the polar
regions and the deep sea.

On the contrary, thermophile is an organism—a type of organism —that

thrives at relatively high temperatures, between 41 and 122 °C. One
like Thermus aquaticus used in PCR.
 The bacterial growth curve represents the number of live cells in a
bacterial population over a period of time.

 Lag Phase: This initial phase is characterized by cellular activity but not

growth. A small group of cells are placed in a nutrient rich medium that
allows them to synthesize proteins and other molecules necessary for
replication. These cells increase in size, but no cell division occurs in
the phase.
 Exponential (Log) Phase: After the lag phase, bacterial cells enter the
exponential or log phase. This is the time when the cells are dividing by
binary fission and doubling in numbers after each generation time.
Metabolic activity is high as DNA, RNA, cell wall components, and other
substances necessary for growth are generated for division. It is in this
growth phase that antibiotics and disinfectants are most effective as
these substances typically target bacteria cell walls or the protein
synthesis processes of DNA transcription and RNA translation.
 Stationary Phase: Eventually, the population growth experienced in the
log phase begins to decline as the available nutrients become depleted
and waste products start to accumulate. Bacterial cell growth reaches a
plateau, or stationary phase, where the number of dividing cells equal
the number of dying cells. This results in no overall population growth.
Under the less favorable conditions, competition for nutrients increases
and the cells become less metabolically active. Spore forming bacteria
produce endospores in this phase and pathogenic bacteria begin to
generate substances (virulence factors) that help them survive harsh
conditions and consequently cause disease.
 Death Phase: As nutrients become less available and waste products
increase, the number of dying cells continues to rise. In the death
 phase, the number of living cells decreases exponentially and
population growth experiences a sharp decline. As dying cells lyse or
break open, they spill their contents into the environment making these
nutrients available to other bacteria. This helps spore producing
bacteria to survive long enough for spore production. Spores are able to
survive the harsh conditions of the death phase and become growing
bacteria when placed in an environment that supports life.

5 kingdom classification charts