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Introduction of Physics

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. {Chapter 1}

Branches of Physics

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1. Consistent Studying and Academic Success:

Consistent studying forms the backbone of academic success by allowing students to gradually build a comprehensive understanding of course materials. Regular engagement with the subject matter reinforces learning, promotes information retention, and helps students develop a strong foundation of knowledge. This approach not only aids in performing well on individual tests but also contributes to a deeper understanding of the overall curriculum, facilitating success in subsequent, more advanced courses.

2. Conceptual Understanding vs. Memorization:

Emphasizing conceptual understanding over mere memorization is essential in effective study habits. When students focus on grasping the underlying principles and relationships within a subject, they develop critical thinking and problem-solving skills. This approach not only prepares them for a broader range of questions on exams but also equips them to apply their knowledge in real-world scenarios. By delving into the core concepts, students cultivate a more profound and lasting understanding that goes beyond the surface-level memorization of facts.

3. The Crucial Role of Time Management:

Time management skills are pivotal in achieving the best academic performance. The ability to allocate time wisely during study sessions, prioritize tasks, and maintain a balanced study routine ensures that students cover all necessary material without feeling rushed or overwhelmed. Effective time management not only enhances productivity but also minimizes stress, allowing students to approach exams with confidence and a well-prepared mindset.

4. Enhancing Learning Through Diverse Resources:

Utilizing a diverse range of study resources significantly enriches the learning experience for students. Textbooks, online materials, educational tools, and supplementary resources provide different perspectives on the same topic, offering a more holistic understanding. Exposure to various resources helps students connect concepts, see practical applications, and adapt their learning style to different formats, ultimately leading to a more comprehensive and nuanced comprehension of the subject matter.

5. Positive Learning Environment through Seeking Help:

Seeking help when faced with challenges not only contributes to individual growth but also fosters a positive and supportive learning environment. When students feel comfortable asking questions and seeking clarification, it creates a collaborative culture where knowledge is shared. This collaborative approach not only helps the struggling student but also benefits the entire class, promoting a sense of community and mutual support. In such an environment, everyone is encouraged to overcome obstacles together, creating a positive and enriching educational experience.

Testing's Role in Achieving the Best Grades:

Tests play a pivotal role in achieving the best grades by serving as comprehensive assessments of a student's understanding and knowledge. Here's how they contribute:

1. Evaluation of Understanding:

Tests assess how well a student has grasped the subject matter. They go beyond memorization, requiring the application of concepts and critical thinking, ensuring a deeper understanding of the material.

2. Identification of Strengths and Weaknesses:

Test results provide valuable feedback, pinpointing areas of strength and weakness. This information allows students to focus their efforts on areas that need improvement, optimizing study strategies for better performance.

3. Motivation and Goal Setting:

The prospect of a test encourages students to stay disciplined and consistently engage with the material. Setting goals for test preparation fosters a proactive approach to studying, leading to more effective learning outcomes.

4. Measuring Progress:

Tests serve as checkpoints to measure academic progress. Regular assessments allow students to track their development, adjusting study techniques as needed to continually enhance their understanding and performance.

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Testing's Role in Achieving the Best Grades:

Tests play a pivotal role in achieving the best grades by serving as comprehensive assessments of a student's understanding and knowledge. Here's how they contribute:

1. Evaluation of Understanding:

2. Identification of Strengths and Weaknesses:

3. Motivation and Goal Setting:

ve learning outcomes.

Physics December Test Sessions

Physics

First Year (class 11)

.December Test Sessions 2023

1. Consistent Studying and Academic Success:

2. Conceptual Understanding vs. Memorization:

3. The Crucial Role of Time Management:

4. Enhancing Learning Through Diverse Resources:

5. Positive Learning Environment through Seeking Help:

Testing's Role in Achieving the Best Grades:

Tests play a pivotal role in achieving the best grades by serving as comprehensive assessments of a student's understanding and knowledge. Here's how they contribute:

1. Evaluation of Understanding:

2. Identification of Strengths and Weaknesses:

3. Motivation and Goal Setting:

4. Measuring Progress:

CHAPTER 2

ENZYMES

MCQs

Encircle the correct choice:

i) Which of the following statements is (are) true about enzyme catalyzed reactions?

(a) The reaction is faster than the same reaction in the absence of the enzyme.

(b) The free energy change of the reaction is opposite from the reaction in the absence of the enzyme.

(d) Both a and b.

ii) The active site of an enzyme is the region that

a) Binds allosteric regulators of the enzyme

b) ( Is involved in the catalytic reaction of the enzyme

c) Binds the products of the catalytic reaction

(d) Is inhibited by the presence of a coenzyme or a cofactor.

(iii) According to the induced fit hypothesis of enzyme catalysis, which of the following is correct?

(a) The binding of the substrate depends on the shape of the active site.

(b) Some enzymes change their structure when activators bind to the enzyme.

c) A competitive inhibitor can outcomepete the substrate for the active site.

(d) The binding of the substrate changes the shape of the enzyme's active site.

iv) Which curve represents the behavior of an enzyme taken from a bacterium that lives in hot-springs.

I. Curve 1 II. Curve 2 III. Curve 3.

(a) I only. (b) II only

(e) II and III

V) Increasing the substrate concentration in an enzymatic reaction could overcome which of the following?

(a) Denaturization of the enzyme

(b) Allosteric inhibition

(d) Saturation of the enzyme activity

Vi) Competitive inhibitors block the entry of substrate into the active site of an enzyme. On which of the following properties of an active site does this primarily depend?

(a) The ability of an enzyme to form a template for holding and joining molecules

(b) The enzyme's ability to stretch reactants and move them toward a transition state

(d) The enzyme forming covalent bonds with the reactants

Vii) A series of enzymes catalyze the reaction XYZ A. Product A binds to the enzyme that converts X to Y at a position remote from its active site. This binding decreases the activity of the enzyme. What is substance X ?

A) A coenzyme. (b) An allosteric inhibitor

c) A substrate. (d) An intermediate

Viii) If an enzyme is added to a solution where its substrate and product are in equilibrium, what would occur ?

(a) Additional product would be formed.

(b) Additional substrate would be formed

(d) Nothing; the reaction would stay at equilibrium.

ix) Which one of the following is the mechanism of action of enzymes?

(a) They act upon substrate molecules to release new substrate molecules

(b) They actually increase the amount of energy of activation.

(d) Enzymes break product molecules to release new product molecules.

X) How does a noncompetitive inhibitor decrease the rate of an enzyme reaction?

(a) By binding at the active site of the enzyme

(b) By changing the shape of a reactant

(d) By acting as a coenzyme for the reaction

MCQs ANSWERS

1. a 2. b 3. a 4. C

5. C 6. a 7. C 8. C

9. a 10. b

SHORT QUESTIONS

Write short answers of the following question:

i) Why enzymes are specific in nature?

SPECIFITY OF ENZYMES:-

We can loosely speak of enzymes and their substrates (the chemicals they act on) as being like a lock and key. The enzyme has a specific lumpy surface shape with some pockets called active sites that can receive the substrate, like a lock that can receive only one specific key.

ii. Why enzymes activity is directly proportional to enzymes concentration ?

In most situations, decreasing enzyme concentration has a direct influence on enzyme activity because each enzyme molecule is able to catalyse only one reaction at a time. The molecule to which an enzyme binds is called a substrate. In general, one enzyme binds to one substrate in order to lower the activation energy for one chemical reaction. If all the enzymes in a system are bound to substrates, additional substrate molecules must wait for an enzyme to become available following the completion of a reaction. This means that the rate of reactions will decrease as enzyme concentration decreases.

iii. Why enzymes are called temperature sensitive ?

ENZYMES ARE TEMPERATURE SENSITIVE :-

The proteins in enzymes are usually globular. The intra- and intermolecular bonds that hold proteins in their secondary and tertiary structures are disrupted by changes in temperature and pH. This affects shapes and so the catalytic activity of an enzyme is pH and temperature sensitive.

iv) How enzymes reduce the energy of activation ?

Ans: Enzymes reduce the energy of activation by reacting with energy rich and energy poor molecules to form an intermediate complex this complex again breaks into product and enzyme.

If activation of this complex is low many molecules can participate in reaction in this way activation energy is lowered

v. How enzymes activity effect on substrate concentration?

EFFECT ON SUBSTRATE CONCENTRATION :-

An increase in substrate concentration leads to an increase in the rate of an enzyme- catalyzed reaction. As the enzyme molecules become saturated with substrate, this increases in reaction rate levels off. The rate of an enzyme-catalyzed reaction increases with an increase in the concentration of an enzyme.

vi. What do you mean by prosthetic group?

PROSTHETIC GROUP :-

A prosthetic group is a tightly bound, specific non-polypeptide unit required for the biological function of some proteins. The prosthetic group may be organic (such as a vitamin, sugar, or lipid) or inorganic (such as a metal ion), but is not composed of amino acids.

vii. Differentiate between inhibitors and activators.

LONG QUESTIONS

Write detailed answers of the following questions:

1..What enzymes explain characteristics of enzymes.

Ans… An enzyme is a type of protein that catalyzes chemical reactions in the body. There are many different types of enzymes that serve a variety of functions, such as digesting food, synthesizing hormones, and repairing DNA.

Five Characteristics of enzymes :-

1_ Enzymes are highly specific, meaning that each enzyme catalyzes a specific reaction or set of reactions.

2_ Enzymes are efficient, meaning that they can catalyze large numbers of reactions in a short period of time.

3_ Enzymes are reversible, meaning that they can catalyze both the forward and reverse reactions of a chemical reaction.

4_ Enzymes are regulated, meaning that their activity can be turned on or off by various signals within the body.

5_ Enzymes are sensitive to their environment, meaning that their activity can be affected by factors such as temperature, pH, and the presence of other

2.. Describe the effect if temperature on the rate of enzyme action.

Ans_ The rate of enzyme action is significantly affected by temperature. Enzymes are biological catalysts that speed up chemical reactions within living organisms by lowering the activation energy required for the reaction to occur. However, like most biological processes, enzyme activity is sensitive to changes in temperature.

The general relationship between temperature and enzyme activity follows a bell-shaped curve known as the temperature-activity profile. At low temperatures, enzyme activity is typically low, as the molecules have less kinetic energy and move more slowly, resulting in fewer collisions between the enzyme and the substrate. As the temperature increases, enzyme activity also increases due to the higher molecular motion, leading to more frequent collisions and a greater likelihood of successful interactions between the enzyme and the substrate.

n is an optimal temperature at which enzymes exhibit their maximum activity, known as the optimum temperature. At this point, the enzyme's active site is in its most flexible and active state, allowing it to bind to the substrate efficiently and catalyze the reaction at the highest rate. This optimal temperature varies for different enzymes and is often around human body temperature, approximately 37°C (98.6°F) for many enzymes involved in human metabolism.

However, as the temperature continues to rise above the optimum, the enzyme's structure becomes increasingly unstable. The increased molecular motion causes the enzyme's three-dimensional structure to break down or denature, resulting in a loss of its catalytic activity. Denaturation occurs because the high temperature disrupts the weak bonds, such as hydrogen bonds and van der Waals forces, that maintain the enzyme's shape.

Consequently, enzyme activity rapidly declines as the temperature exceeds the optimum, and the enzyme eventually becomes completely inactive. This decline is often depicted as a steep drop on the temperature-activity profile after the optimum temperature. Extremely high temperatures can even cause irreversible damage to the enzyme structure, rendering it permanently non-functional.

It is important to note that different enzymes have different temperature optima and stability ranges, depending on their natural habitat and biological function. Some enzymes, such as those found in thermophilic bacteria living in hot springs, have higher temperature optima and greater stability at elevated temperatures compared to enzymes from organisms that thrive in moderate or cooler environments.

In summary, while enzymes demonstrate increased activity with rising temperature up to their optimum, excessive heat can lead to denaturation and loss of enzymatic function. Understanding the relationship between temperature and enzyme activity is crucial for various fields, including biochemistry, biotechnology, and medicine, as it helps optimize enzyme-based reactions and ensures proper functioning of biological Systems.

3. Describe mechanism of enzyme action.

Ans: Enzymes are proteins that catalyze chemical reactions in living organisms. They work by lowering the activation energy required for a reaction to occur, which allows the reaction to proceed more rapidly and efficiently.

Enzymes do this by providing an alternative reaction pathway with a lower activation energy. They do this by bringing the reactant molecules into close proximity with each other, and by temporarily binding to them in a way that helps to stabilize the intermediate states that are formed during the reaction.

The active site of an enzyme is the region where the substrate binds and the chemical reaction occurs. The shape of the active site is complementary to the shape of the substrate, which allows the substrate to fit into the active site like a lock into a key. This close fit between the substrate and the active site helps to bring the reactant molecules into close proximity and facilitates the chemical reaction.

Enzymes can be regulated by various means, such as through the presence or absence of certain chemical inhibitors or activators, or through changes in the enzyme's environment, such as pH or temperature.

4. Describe the classification of enzymes

Ans: Enzymes are proteins that catalyze chemical reactions in living organisms. They are classified into six main categories based on the type of reaction they catalyze:

Oxidoreductases:

Enzymes that catalyze oxidation-reduction reactions, such as the transfer of electrons from one molecule to another.

Transferases:

Enzymes that transfer chemical groups from one molecule.

to another.

Hydrolases:

Enzymes that catalyze the hydrolysis of chemical bonds, typically by adding a water molecule to break the bond.

Lyases:

Enzymes that cleave chemical bonds by means other than hydrolysis and oxidation, such as by the removal of a small molecule.

Isomerases:

Enzymes that catalyze the rearrangement of atoms within a molecule to form a different isomer

Ligases:

Enzymes that catalyze the formation of a chemical bond by joining two molecules together, often with the simultaneous hydrolysis of ATP or a similar molecule.

Enzymes are often further classified by the type of substrate they act on and the type of reaction they catalyze. For example, an enzyme that breaks down proteins is called a protease, and an enzyme that synthesizes DNA is called a DNA polymerase

5. Describe enzymatic inhibition, its types and significance.

Ans: Enzyme inhibition is the reduction of enzyme activity. This can be a temporary or permanent effect. Enzyme inhibitors can be classified into several types, including:

Competitive inhibitors

These molecules compete with the substrate for binding to the enzyme active site. They have a similar shape to the substrate and can bind to the active site, but do not undergo a chemical reaction. This blocks the substrate from binding and reduces the. overall activity of the enzyme.

Non-competitive inhibitors:

These molecules bind to the enzyme at a site other than the active site. This can cause a change in the conformation of the enzyme, which can prevent the substrate from binding to the active site or can prevent the enzyme from properly catalyzing the reaction.

Uncompetitive inhibitors:

These inhibitors bind to the enzyme-substrate complex, preventing the reaction from occurring.

Enzyme inhibition is significant because it is a key regulatory mechanism in biological systems. Enzyme inhibitors can be used to modulate the activity of enzymes, which can have therapeutic implications. For example, many drugs work by inhibiting enzymes involved in disease processes. Inhibiting the activity of these enzymes can help to control the disease and improve the symptoms of the patient.

6. Describe structure of enzymes.

Ans: An enzyme is a protein that catalyzes chemical reactions in the body. Enzymes are highly specific and can only catalyze a single reaction or a specific set of reactions.

The structure of an enzyme can be divided into two main parts: the active site and the remainder of the enzyme.

The active site is the region of the enzyme that binds to the substrate (the molecule that the enzyme acts on). The active site is usually a depression or cleft on the surface of the enzyme, and it is lined with amino acid residues that help to bind and stabilize the substrate.

The remainder of the enzyme is made up of the protein chain that surrounds the active site. This part of the enzyme helps to hold the active site in the correct conformation for catalysis and may also help to stabilize the substrate as it is being converted.

Overall, the structure of an enzyme is important because it determines the enzyme's activity and specificity. The specific arrangement of amino acid residues in the active site allows the enzyme to bind to and recognize its substrate, while the remainder of the enzyme helps to maintain the proper conformation of the active site.

7. Explain the effect of substrate and concentration on the rate of enzyme action.

The substrate and its concentration play crucial roles in determining the rate of enzyme action. Enzymes are biological catalysts that facilitate chemical reactions by binding to specific substrates. Here's a short explanation of their effects:

1. Substrate: The substrate is the molecule that an enzyme acts upon. Enzymes have specific binding sites, known as active sites, where substrates bind and undergo a chemical reaction. The presence or absence of a suitable substrate directly affects the rate of enzyme action. Without a substrate, the enzyme remains inactive.

2. Concentration: The concentration of the substrate refers to the amount of substrate molecules present in a given volume. The concentration of the substrate can significantly influence the rate of enzyme action. As the substrate concentration increases, the rate of the enzyme-catalyzed reaction generally increases until it reaches a maximum point.

At low substrate concentrations, the enzyme may not encounter enough substrate molecules, leading to a slower rate of reaction. This occurs because the enzyme's active sites are not fully occupied. As the substrate concentration increases, more active sites become engaged, resulting in a higher rate of reaction.

However, once the maximum rate is achieved, further increases in substrate concentration do not have a significant effect on the rate of enzyme action. This is because all the active sites are already saturated with substrate, and the enzyme is functioning at its maximum capacity.

In summary, the substrate is necessary for enzyme action, and its concentration affects the rate of the reaction. Low substrate concentrations result in slower reactions, while higher concentrations increase the reaction rate until reaching a plateau where further increases have minimal impact.

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About BIEK:

The Board of Intermediate Education Karachi (BIEK) is a prominent educational institution in Pakistan, primarily responsible for overseeing and conducting intermediate-level examinations within the Karachi region. Established in 1974, BIEK plays a crucial role in shaping the educational landscape of the Sindh province. Its inception marked a significant shift in the education system, as it centralized the examination and evaluation process for intermediate students.

BIEK offers a wide range of academic disciplines, catering to the diverse needs and interests of students. These disciplines encompass science, commerce, humanities, and vocational subjects, allowing students to pursue their chosen career paths effectively.

Throughout its history, BIEK has evolved to meet the changing demands of education in Karachi. It has adopted modern technologies for examination management, result dissemination, and student services, ensuring transparency and efficiency in its operations.

BIEK's commitment to educational excellence and its role in facilitating the transition of students from secondary to higher education has contributed significantly to the academic development of Karachi's youth. With a focus on quality education and rigorous assessment, BIEK continues to play a pivotal role in shaping the future of thousands of students in the Karachi region.

Section B CRQ's

Section B

CRQ's

1. Give an example of (1) a physical quantity which has a unit but no dimensions. (II) a physical quantity which has neither unit not dimensions. (III) a constant which has a unit. (IV) a constant which has no unit.

Ans..

I. Physical quantity with a unit but no dimensions: Planar angle in radians. It's a unit of angle measurement and doesn't have any dimensions.

II. Physical quantity with neither unit nor dimensions: Pure number, like the coefficient in a dimensionless quantity such as the coefficient of friction or the fine-structure constant in physics.

III. Constant with a unit: Avogadro's number (6.022 x 10^23 mol^-1) is a constant with the unit "per mole."

IV. Constant with no unit: The mathematical constant π (pi) doesn't have any physical unit associated with it.

2. When rounding the product or quotient of two measurements, is it necessary to consider Significant digit ?

Ans.. Yes, when rounding the product or quotient of two measurements, it's important to consider significant digits. The result should be rounded to the same number of significant digits as the measurement with the fewest significant digits. This helps maintain the accuracy and precision of the calculated value and ensures that the final result reflects the limitations of the original measurements.

5. You measure the radius of a wheel to be 4.16 cm. If you multiply by 2 to get diameter, should you write the result as 8 cm or as 8.32 cm? Justify your answer.

Ans

Formula for the relation between the radius and diameter of a circle

Given Data:

The radius of the wheel (R) is 4.16 cm

The diameter is a line segment that passes through the center of a circle and touches the circumference of the circle with its endpoints.

The formula for the diameter of a wheel is

D= 2R...... (I)

Calculating the radius of the wheel

To find the diameter, take the value of radius in equation (i).

Thus, you have

D= 2 × 4.16D = 8.32 cm

The calculated value of the diameter is 8.32 cm.

The value of radius 4.16 cm has three significant digits. By the rules of significant digits, the diameter must also have three significant digits.

The value 8 cm has only one significant digit. In comparison, 8.32 cm has three significant digits, equal to those in 4.16 cm. Therefore, 8.32 cm is the more accurate value of the diameter.

6. If y=a+bt+ct where y is in meters and t in seconds, what is the unit of c?

Solution

Dimension of a,bt,ct2 should be equal to x

x=[L]

So, the dimension of bt will be equal to that of 'x'

b t=[L]

b=[T][L]

b=[LT−1]

The dimension of c can be obtained as:

ct2=[L]

c=[T2][L]

c=[LT−2]

7. Differentiate between accuracy and precision

Ans...

8. Define dependent and independent variables

Ans...

A1. Dependent variable:

A variable that is being measured or observed in an experiment or study, and is expected to change as a result of the manipulation of the independent variable.

Independent variable: A variable that is manipulated in an experiment or study to observe the effect it has on a dependent variable. It's also referred to as the predictor variable, explanatory variable, or input variable.

9. Differentiate systematic error and random error.

Ans...

11. Describe least count of Vernier and screw gauge micrometer.

The least count of a measuring instrument is the smallest measurement that can be accurately recorded by that instrument.

In a Vernier caliper, the least count is the difference between one main scale division and one Vernier scale division. It helps in obtaining more precise measurements by reading both scales.

For a screw gauge micrometer, the least count is determined by the pitch of the screw and the number of divisions on the circular scale. It's the smallest distance the screw can move, which corresponds to one division on the circular scale.

The formulas to calculate the least count are:

- For Vernier caliper: Least Count = Value of one main scale division - Value of one Vernier scale division.

- For screw gauge micrometer : Least Count = Pitch of screw / Number of divisions on the circular scale.

These least counts contribute to the precision of measurements made using these instruments.

12... Describe extrapolation methods

Extrapolation: Estimating Beyond Observed Data:

Extrapolation is a statistical technique involving the estimation of values beyond the scope of collected data. It entails predicting future or unobserved data by identifying trends or patterns in existing data.

Method of Extrapolation: Projecting Trends

Extrapolation involves extending known trends or patterns from existing data to make predictions about unseen data. For instance, consider a volume-temperature graph where extending a line until it intersects the temperature axis predicts a zero Kelvin temperature.

Key Concept: Using Existing Patterns

The core idea of extrapolation is utilizing established data patterns to anticipate outcomes that lie beyond the range of available data.

Summary: Predicting Unseen Data

In summary, extrapolation is a valuable statistical tool to make educated guesses about future or unobserved data based on patterns identified within existing data.

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The Board of Intermediate Education Karachi (BIEK) stands as a vital institution in the landscape of education in Pakistan. Established to oversee intermediate education in Karachi, the BIEK plays a pivotal role in shaping the academic journey of students transitioning from school to higher education. With a rich history and a commitment to excellence, the board serves as a guiding force for thousands of students each year.

BIEK, also known as the Karachi Inter Board, operates as an autonomous body that governs and regulates intermediate education within the jurisdiction of Karachi. Its mandate extends to affiliating educational institutions, designing curricula, conducting examinations, and ensuring the overall standard of education at the intermediate level. The board's scope covers a wide range of disciplines, including humanities, sciences, commerce, and the arts.

One of BIEK's significant responsibilities lies in the organization and execution of intermediate examinations. These examinations hold immense importance as they serve as a bridge between school education and university-level studies. The credibility and transparency maintained in these examinations reflect the board's commitment to fair evaluation and accurate assessment of students' knowledge and abilities.

BIEK's efforts extend beyond examinations. The board consistently strives to enhance the quality of education by revising curricula to align with contemporary trends and requirements. It endeavors to equip students with the skills and knowledge needed to excel not only academically but also in their future endeavors.

Moreover, BIEK serves as a platform that nurtures students' potential and fosters their personal growth. The board encourages extracurricular activities, such as debates, sports, and arts, alongside academics, creating a well-rounded educational experience for students.

In conclusion, the Board of Intermediate Education Karachi (BIEK) embodies the essence of educational development and progression. With a legacy of excellence, it stands as a cornerstone of the educational system in Karachi. Through its dedication to fostering academic growth, promoting integrity, and shaping well-rounded individuals, BIEK plays a transformative role in the lives of countless students, preparing them to contribute meaningfully to society and the world at large.

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Biology Class 11 Chapter 9

Biology Class 11 Chapter 10

Biology Class 11 Chapter. 11

Biology Class 11 Chapter 12

Biology Class 11 Chapter

Biology Class 12 Chapter

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