Biological+Molecules

Stearic acid.

Condensation reaction.

A water molecule.

A covalent bond known as a peptide bond.

'Mer' refers to pieces.

A hydroxyl group from the carboxyl end of one amino acid and a hydrogen from the amino group of another amino acid.

A dinucleotide.

Condensation reactions involve the joining of monomers to form polymers, releasing water as a byproduct.

It induces a conformational change in the enzyme's active site.

Molecules that consist of multiple monomers.

Mostly in plant oils and fish fats.

It suggests that enzymes and substrates fit together perfectly, like a key in a lock.

Glycogen is more branched than amylopectin.

Through hydrolysis.

Deoxyribose.

To the 1st carbon of the pentose sugar.

Below the ring plane.

Induced-fit model.

Violet.

Temperature can increase the rate of enzyme activity up to an optimal point, beyond which the enzyme may denature.

The peptide bond is broken down.

Yes, enzymes can catalyze both reversible and irreversible reactions.

20 types.

Cytosine (C), Uracil (U), and Thymine (T).

Polymers that are key components of every living cell.

It is essentially the reverse of the dehydration reaction.

Phosphodiester bond.

A slight change in the shape of the enzyme is induced.

From 5’ to 3’.

Saturated fatty acids have no double bonds, while unsaturated fatty acids contain one or more double bonds.

Condensation process.

It emphasizes a rigid structure where the enzyme's active site is complementary to the substrate.

The carbonyl group is located at the end of the carbon chain.

The sequence of amino acids in a polypeptide chain.

Carbohydrates serve as a primary energy source and structural components.

They consist of a single sugar unit, typically with a formula of (CH2O)n.

It falls out of solution, resulting in a cloudy white emulsion.

A single protein formed when two or more polypeptide chains join.

Phosphodiester bond.

The induced fit model and the lock and key hypothesis.

Triacylglycerol.

A polynucleotide.

The assembly of multiple polypeptide chains into a single functional unit.

α-glucose.

The arrangement of protein structure from primary to quaternary levels.

Enzymes are proteins that catalyze biochemical reactions.

Uracil (U).

Nitrogenous base, pentose sugar, and phosphate group.

They are arranged in opposite directions (antiparallel).

It forms an enzyme-substrate complex.

A carbohydrate made up of two sugar units.

Monosaccharides, disaccharides, and polysaccharides.

Repeating sugar-phosphate units.

Sweet, soluble in water, can crystallize, and are white/colorless.

DNA is a polynucleotide, which is a polymer of nucleotides.

The formation of hydrogen bonds between the backbones of amino acids.

To carry out its catalytic function.

They are solid at room temperature.

Enzymes are specific to their substrate.

Glucose.

A positive test for proteins.

Lipids are used for energy storage, insulation, and making up cell membranes.

They are formed by the combination of two monosaccharides through a glycosidic bond.

Single ring.

A polymer is a large molecule made up of repeating monomer units.

Peptide bond.

Enzymes are proteins that catalyze biochemical reactions.

They have both acidic and basic properties.

The active site is not flexible and is exactly complementary to the substrate.

Through 3 condensation reactions, also known as esterification.

Reducing sugars.

α-1,4 glycosidic bond and α-1,6 glycosidic bond.

Structural support.

The lock and key hypothesis assumes a rigid fit, while the induced fit model allows for flexibility and adaptation of the enzyme's active site.

The model where the enzyme changes shape to fit the substrate upon binding.

The active site is not exactly complementary to the substrate.

Products are not complementary with the active site of the enzyme.

The complementary shape of the active site and the substrate.

Proteins, Carbohydrates, Lipids, and Nucleic acids.

The overall three-dimensional shape of a protein formed by the folding of its polypeptide chains.

The Induced Fit model proposes that the enzyme changes shape to better fit the substrate upon binding.

The active site changes shape to become fully complementary with the substrate.

Hydrolysis.

Glycosidic bond.

A dinucleotide.

Blue.

α-glucose and β-glucose.

They differ in their side chain (R group).

Higher enzyme concentration typically increases the reaction rate, provided there is enough substrate available.

Fatty acids that can be synthesized in the body, such as stearic acid.

Proteins function as enzymes, structural components, and signaling molecules.

Malt sugar.

It is helical and forms an unbranched chain of α-glucose.

3 fatty acids and 1 glycerol backbone.

Double rings.

It consists of two polynucleotide chains twisted to form a double helix.

Energy storage.

The bonds are broken, causing it to uncoil and change its conformation.

Enzyme.

COOH group.

A genetic disorder that affects the shape of red blood cells.

Lipids are used for energy storage, insulation, and making up cell membranes.

3 to 7 carbon atoms.

The specific monomer is not provided in the text.

'Poly' means many.

Ribose.

Above the ring plane.

Energy storage in the liver and muscle.

The active site of the enzyme is exactly complementary to the substrate.

Explaining the structure of DNA and identifying structural components from diagrams.

Induced fit model and lock and key hypothesis.

Polymers are large molecules formed by the linking of multiple monomers.

Each enzyme has an optimal pH range; deviations can reduce activity or denature the enzyme.

A chemical reaction where two molecules combine to form a larger molecule, releasing water.

A bond formed between monosaccharides during polymerization.

The hydrophilic (water-attracting) phosphate head interacts with water, while the hydrophobic (water-repelling) fatty acid tails repel water, allowing phospholipids to form bilayers in cell membranes.

Saturated fatty acids have no double bonds between carbon atoms, while unsaturated fatty acids have one or more double bonds.

They are the basic building units or monomers.

Carbon (C), Hydrogen (H), Oxygen (O), Phosphorus (P), and Nitrogen (N).

Fats that consist of saturated fatty acids, commonly known as saturated fat.

The simplest form of carbohydrates, consisting of single sugar molecules.

Monosaccharides, disaccharides, and polysaccharides.

Due to the bending caused by double bonds.

They are long chains of monosaccharide units linked by glycosidic bonds.

A color change to cloudy white.

The coiling of a polypeptide chain into a globular shape maintained by bonds and interactions among R groups.

An amino acid consists of a central carbon atom, an amino group, a carboxyl group, a hydrogen atom, and a variable R group.

Silk and spider web.

Nucleotides.

1 glycerol and 3 fatty acids.

Condensation reactions build polymers, while hydrolysis reactions break them down.

The substrate is the 'key' that fits exactly into the 'lock' (enzyme).

C6H12O6

In small quantity.

The substrate can no longer fit into the active site, inhibiting enzyme function.

A functional group with the structure C=O.

Primary, Secondary, Tertiary, and Quaternary.

Non-polar, Basic, Polar, Acidic.

An alkaline solution of copper (II) sulfate.

A reaction that forms polymers by joining monomers and releasing water.

Serine.

Polymerization of α-glucose.

Adenine (A) and Guanine (G).

A widely accepted hypothesis stating that the enzyme's active site changes shape to better fit the substrate upon binding.

It has a zig-zag pattern.

By observing the color change in the solution.

Condensation forms polymers, while hydrolysis breaks them down.

Amino acids that cannot be synthesized in sufficient amounts and must be obtained through food or supplements.

Adenine with Thymine, and Cytosine with Guanine.

Increased kinetic energy causes protein atoms to vibrate, breaking H & ionic bonds and van der Waals interactions.

A 5-carbon sugar.

Carbohydrates serve as a primary energy source and structural components.

A hydrogen atom, a carboxyl group, an amino group, and a variable R group (or side chain).

It consists of a central carbon (C), an amino group (NH2), a carboxyl group (COOH), a hydrogen atom (H), and a variable R group.

The active site is flexible and not exactly complementary to the substrate.

It describes how the attachment of substrates induces a conformational change in the active site of the enzyme, allowing it to fit the substrate.

Fibrous, globular, and conjugated.

Hydrolysis is the process of breaking down polymers into monomers by adding water.

It is not fully complementary to the shape of the substrate.

Polynucleotide.

All carbon atoms are clearly shown.

Glycerine.

The lock and key model.

Because of their straight chain structure.

The induced fit model and the lock and key model.

By facilitating the breaking and formation of bonds in the substrate.

No color change or a blue color.

Alpha helix and beta pleated sheet.

The enzyme changes back to its original conformation.

A reaction that breaks down polymers into monomers by adding water.

pH and temperature.

The carbonyl group is located in the middle of the carbon chain.

The minimum amount of energy required by a reactant (substrate) to start a chemical reaction.

Uracil.

The minimum energy required for a reaction to occur.

Starch and glycogen are formed from α-glucose, while cellulose is formed from β-glucose.

Glycine.

They form the genetic code by pairing with complementary bases.

Hemoglobin, which consists of 4 polypeptide chains (two α chains and two β chains).

The active site of the enzyme is specifically shaped to fit the substrate.

Peptide bonds.

Four types of interactions between R groups.

Pentose sugar, phosphate group, and nitrogenous base.

The linear sequence of amino acids joined by peptide bonds within a polypeptide chain.

A type of monosaccharide with an aldehyde functional group.

Monomers are the basic building blocks of polymers.

B) Condensation

3 molecules of water (H2O).

Ester bonds.

Deoxyribonucleic Acid (DNA) and Ribonucleic Acid (RNA).

Iodine solution.

The type of pentose sugar: deoxyribose in DNA and ribose in RNA.

C18H36O2.

Phospholipids consist of a glycerol backbone, two fatty acid tails, and a phosphate group.

To detect the presence of lipids in a solution.

Nucleotides.

Guanine, Adenine, Thymine, Cytosine.

Saturated and Unsaturated.

Aspartic acid.

Monomers are the basic building blocks of polymers.

The overall three-dimensional shape formed by the interactions between R groups of amino acids.

Based on the properties of their R group.

The Induced Fit Model involves a change in the enzyme's shape to accommodate the substrate, while the Lock and Key Model does not.

Saturated fatty acids have no double bonds, while unsaturated fatty acids have one or more double bonds.

Reducing and non-reducing sugars.

Carbohydrates formed by the combination of two monosaccharides.

Because it is very compact due to its folded structure.

8 essential amino acids.

It begins with the carbon nearest to the carbonyl group.

RNA nucleotide.

It determines the protein's overall shape and function.

The simplest form of carbohydrates, consisting of single sugar molecules.

An enzyme-substrate complex is formed.

By phosphodiester bonds.

Glyceraldehyde or dihydroxyacetone.

Proteins function as enzymes, structural components, and signaling molecules.

The specific name of the polysaccharide is not provided in the text.

Two amino acids are joined by a condensation process.

A dehydration reaction.

Condensation reaction.

Deoxyribose.

α-glucose (below the ring plane) and β-glucose (above the ring plane).

A 3’ hydroxyl group.

A 5’ phosphate group.

Globular protein.

To the 5th carbon of the pentose sugar.

Hydrolysis.

Oleic acid.

Monomers are the basic building blocks of polymers.

Paired inside the helix.

Polymers are made up of multiple monomers.

Carbon, hydrogen, and oxygen atoms.

A blue-black coloration.

Pyrimidine and Purine.

The tertiary structure determines the shape of the active site, which is crucial for substrate binding.

Monosaccharides, disaccharides, and polysaccharides.

By joining two monosaccharides through a condensation process (removal of a water molecule).

Two amino acids.

Fatty acids that cannot be synthesized in the body and must be present in the diet, such as linoleic, linolenic, and arachidonic acids.

Saturated fatty acids have no double bonds, while unsaturated fatty acids have one or more double bonds.

Polymerization of α-glucose.

A fatty acid with no double bonds between carbon atoms, fully saturated with hydrogen.

The folding or coiling of the polypeptide chain into alpha-helices or beta-pleated sheets.

They bind at the enzyme's active site.

A monomer is a small, basic molecular unit that can join together to form polymers.

Nucleotides.

They have no double bonds between carbon atoms.

Fats that consist of unsaturated fatty acids, commonly found in plants and fish.

They have double bonds between carbon atoms.

They have the maximum number of hydrogen atoms.

They speed up the rate of chemical reactions.

A glycerol backbone with three fatty acid chains.

The carbon atoms are omitted.

To test for the presence of proteins.

A 3C alcohol with 3 OH groups, making it soluble in water.

Two drops.

They form long parallel filaments or strands.

It describes how the active site of an enzyme is exactly complementary to its substrate.

A chemical reaction where a larger molecule is broken down into smaller molecules by the addition of water.

α-1,4 glycosidic bond.

Guanine, Adenine, Uracil, Cytosine.

A substance produced by living cells that speeds up the rate of chemical reactions.

Add ethanol to the solution you want to test.

The same as those in the tertiary structure.

Polymers are large molecules formed by the linking of multiple monomers.

Fructose.

Products.

It determines the protein's function and properties.

Saturated fatty acids have no double bonds between carbon atoms, while unsaturated fatty acids have one or more double bonds.

Amphipathic molecules.

Monomers are the basic building blocks of polymers.

Water is removed by extracting OH from the carboxyl group of fatty acids and H from the glycerol’s hydroxyl group.

3 hydrogen bonds.

Mainly carbon and hydrogen atoms, with few oxygen atoms.

Carbohydrates consist of carbon, hydrogen, and oxygen, typically in a ratio of 1:2:1.

It implies that enzymes are flexible and can adapt their shape to accommodate substrates.

The substrate reacts, and the product is released.

10 base pairs.

They facilitate transport.

A carbohydrate consisting of one sugar unit.

An enzyme-substrate complex.

Sugar-phosphate.

They have a straight chain structure.

An amino acid consists of an amino group, a carboxyl group, a hydrogen atom, and a variable side chain (R).

It includes primary, secondary, tertiary, and quaternary structures.

5' to 3' and 3' to 5'.

The hydrogen atoms are omitted.

Approximately 1:2:1 (CH₂O)n.

It determines the protein's function and interaction with other molecules.

Amino acids.

A color change to purple.

Hydrophobic tails.

Hydrogen bonds between complementary base pairs.

Simple sugars consisting of 1 sugar molecule with 3 to 7 carbon atoms.

Lysine.

Saturated fatty acids have no double bonds between carbon atoms, while unsaturated fatty acids have one or more double bonds.

A helical coil formed by hydrogen bonds.

The substrate binds to the active site of the enzyme.

Saturated fatty acids.

The Induced Fit model suggests that the enzyme changes shape to better fit the substrate upon binding.

2 hydrogen bonds.

The energy required to initiate a chemical reaction.

They lower the activation energy needed for the reaction to occur.

Hydrolysis.

Four polypeptide chains.

Starch.

DNA nucleotide.

Polymers are large molecules made up of repeating monomer units.

C-terminal and N-terminal.

A bond formed between monosaccharides during polymerization.

Deoxyribose has one H atom at the 2nd carbon atom, while ribose has one OH group.

It repels water and does not interact well with it.

The shape of the active site is changed, preventing the substrate from fitting.

Hydrolysis (addition of water).

A carbohydrate composed of many sugar units.

They serve as an energy source.

Copper(II) sulfate.

A type of covalent bond that connects carbohydrate molecules through a condensation reaction.

1 Glycerol and 3 Fatty acids.

It implies that enzymes are flexible and can adapt their shape to accommodate the substrate.

The OH group in the phosphate group of one nucleotide and the OH group at the 3rd carbon in the pentose sugar of the other nucleotide.

Saturated fatty acids have no double bonds, while unsaturated fatty acids have one or more double bonds.

At optimum temperature and pH.

Hydrogen bonds between the H of NH groups and the O of C=O groups.

Polymerization of β-glucose.

Through hydrolysis (addition of a water molecule).

Usually 16 or 18.

The linear chain of amino acids.

They speed up the rate of reactions by lowering the activation energy.

Two α-glucose molecules.

They are liquid.

Nucleic acids store and transmit genetic information.

Mostly tertiary/quaternary structure.

Peptide bond.

Monosaccharides.

In cell membranes.

Two monosaccharides linked together by a glycosidic bond.

ATP (adenosine triphosphate) is the primary energy carrier in cells.

A glycoprotein found in saliva that serves as a lubricant.

Starch, glycogen, cellulose, amylose, and amylopectin.

They do not change and are reusable.

Mostly secondary structure.

By lowering the activation energy (E A).

Nucleotides.

Glucose.

A hypothesis suggesting that the enzyme's active site is a perfect fit for the substrate, like a key fits into a lock.

A glycosidic bond.

Insoluble.

A fatty acid that contains one or more double bonds between carbon atoms.

Amino group (NH2) and carboxyl group (COOH).

Inhibitors can decrease enzyme activity by binding to the enzyme or substrate, preventing the reaction.

Proteins function as enzymes, structural components, and signaling molecules.

It provides strength and flexibility.

The substrate.

Thousands or more reactions in a second.

It proposes that the enzyme's active site changes shape to better fit the substrate upon binding, enhancing the reaction.

β - 1,4 glycosidic bond.

Between the first amino acid and the fourth amino acid away from it.

No color change or a clear solution, indicating lipids are absent.

By converting it into starch for storage in chloroplasts.

Isoleucine, leucine, lysine, methionine.

A very stable and tough structure that provides support.

Elasticity, as it can stretch under tension.

A condensation reaction is a process where monomers join together, releasing water and forming a polymer.

Primary, Secondary, Tertiary, and Quaternary.

Usually irreversible, but sometimes renaturation may occur.

Relatively unstable.

Carbohydrates serve as a primary energy source and structural components.

Polymers are large molecules formed by the linking of many monomers.

They can alter enzyme shape and activity, affecting reaction rates.

Cellulose.

It allows the enzyme to bind to its specific substrate.

Increasing substrate concentration generally increases the rate of reaction until the enzyme becomes saturated.

Add an equal volume of Benedict's reagent to the sample.

It suggests that each enzyme is specific to a particular substrate due to the precise fit.

It causes bending in the structure.

The enzyme.

1 Glycerol, 2 Fatty acids, and a Phosphate group.

Mechanical and structural support.

Because it is maintained by weak ionic bonds, hydrogen bonds, and hydrophobic interactions.

They are small, sweet, soluble in water, can crystallize, and are white or colorless.

Condensation process.

Examples include proteins, nucleic acids, and polysaccharides.

Stearic acid (stearate), C18H36O2.

Energy storage and providing structural support.

α-1,4 glycosidic bond.

Polymerization of β-glucose.

Monosaccharides, disaccharides, and polysaccharides.

Fats, phospholipids, and steroids.

Compact spherical shape.

A repeated sequence of (-N-C-C-).

ATP (adenosine triphosphate) is the primary energy carrier in cells.

Histidine.

A variable side chain that determines the specific properties of the amino acid.

ES.

It suggests high specificity, as only substrates that fit the active site can bind.

5' to 3' direction indicates the orientation of the DNA strands.

Cellulose.

It includes primary, secondary, tertiary, and quaternary structures.

Phospholipids consist of a glycerol backbone, two fatty acid tails, and a phosphate group, allowing them to form bilayers in cell membranes.

Glycosidic bond.

Metabolic and chemical processes.

Polymerisation of α-glucose results in long chains that can branch, forming starch or glycogen.

Molecules with the same molecular formulas but different arrangements of atoms.

Enzymes, antibodies, hormones, hemoglobin.

The number of carbon atoms.

Phospholipids form the fundamental structure of cell membranes, creating a barrier that separates the interior of the cell from the external environment.

For 5 minutes.

The sequence of amino acids in a polypeptide chain.

It suggests that the enzyme's active site is exactly shaped to fit a specific substrate, like a key fits into a lock.

Because they have both hydrophilic and hydrophobic regions, allowing them to interact with both water and lipid environments.

They are arranged parallel to one another.

Maltose, sucrose, and lactose.

Water (H2O).

Keratin and collagen.

By hydrogen bonds, forming microfibrils.

Triose (3 C), Pentose (5 C), and Hexose (6 C).

It explains how enzymes can be flexible and adapt to different substrates, enhancing their catalytic efficiency.

Denaturation.

The position of the functional group.

They create branching in the structure.

They provide protection.

To detect the presence of lipids in a sample.

Water is a solvent for biochemical reactions and helps maintain cell structure.

A type of monosaccharide with a ketone functional group.

Condensation reaction.

Water is a solvent for biochemical reactions and helps maintain cell structure.

Amino acids that can be synthesized in the body.

C5H10O5.

α-glucose molecules.

It posits that the enzyme's active site is specifically shaped to fit a particular substrate without any change in shape.

Cellulose.

Proteins function as enzymes, structural components, and signaling molecules.

It emphasizes the dynamic nature of enzyme-substrate interactions.

Amino acids.

To identify the activation energy.

α - 1,4 glycosidic bond and α - 1,6 glycosidic bond.

By a condensation process, which involves the removal of water molecules.

Condensation.

Polymerization of β-glucose.

It suggests that enzyme activity can be influenced by the binding of the substrate, allowing for a more dynamic interaction.

They can be denatured or destroyed.

A model suggesting that the enzyme's active site is exactly shaped to fit a specific substrate.

Mostly animal fats, such as butter and lard.

Phospholipids, such as lecithin.

The Induced Fit Model.

The specific shape of the enzyme allows it to bind only to certain substrates.

The active site of the enzyme is exactly complementary to the substrate.

Complex carbohydrates made up of long chains of monosaccharide units.

Saturated fatty acids have no double bonds, while unsaturated fatty acids have one or more double bonds.

Amino acids.

It contributes to the acidic properties of the amino acid.

It has one end that is hydrophilic (polar) and another end that is hydrophobic (non-polar).

It has an affinity for water and can interact with it.

The Lock and Key Hypothesis suggests that the active site is a perfect fit for the substrate, while the Induced Fit Model involves a conformational change for a better fit.

The numbers of Adenine equals Thymine (A=T) and the numbers of Guanine equals Cytosine (G=C).

They are hydrophobic molecules and are insoluble in water.

Molecules formed by two amino acids linked by a peptide bond.

Complex carbohydrates made up of long chains of monosaccharide units.

The formation of different bonds between amino acids.

Monosaccharides.

Lipids are used for energy storage, insulation, and making up cell membranes.

Amylose and amylopectin.

Glycerol and fatty acids.

They enable movement.

It includes primary, secondary, tertiary, and quaternary structures.

Carbohydrates, proteins, nucleic acids.

Starch.

DNA is double-stranded, contains deoxyribose sugar, and uses thymine, while RNA is single-stranded, contains ribose sugar, and uses uracil instead of thymine.

Helical and unbranched.

H & ionic bonds and van der Waals interactions break.

Biological polymers are made up of specific monomers.

Nucleic acids store and transmit genetic information.

Thymine (T).

The induced fit model suggests that the active site changes shape to better fit the substrate upon binding.

C12H22O11.

Disulfide bonds (covalent bonds).

Main energy storage due to a higher number of hydrogen atoms.

By specific DNA code.

The number and type of monomers used to build it.

The binding of the substrate induces conformational changes to the active site of the enzyme.

Hydrolysis, with the help of the amylase enzyme.

It is a long unbranched hydrocarbon chain.

DNA carries genetic information essential for the growth, development, and reproduction of organisms.

α - glucose.

A monosaccharide with 5 carbon atoms.

α-1,4 glycosidic bond and α-1,6 glycosidic bond.

It can regulate enzyme activity by binding molecules that change the enzyme's shape.

Inhibitors can decrease enzyme activity by blocking the active site or altering enzyme shape.

Polymerisation of β-glucose results in straight chains that form cellulose.

They provide better thermal insulation.

They are lipids that are transported in blood plasma and are components of cell membranes.

A protein that contains a non-protein component, such as a metal ion or a carbohydrate.

Galactose is less sweet than glucose.

The hierarchical organization includes primary, secondary, tertiary, and quaternary levels.

Fruit sugar.

β-1,4 glycosidic bond.

Saturated fatty acids have no double bonds, while unsaturated fatty acids have one or more double bonds.

It emphasizes a rigid fit between enzyme and substrate.

ATP (adenosine triphosphate) is the primary energy carrier in cells.

Breakdown of peptide bonds occurs.

Substrate (reactant).

They contribute to the helical structure of amylose.

Ribose.

It contains a carboxyl group (COOH).

Their amphipathic nature allows them to form cell membranes, with hydrophilic heads facing outward and hydrophobic tails facing inward.

Ionic bonds.

Deoxyribose.

It allows for the determination of the frequency of certain bases based on the frequency of others.

Product.

It allows for a broader range of substrates to interact with the enzyme, enhancing catalytic efficiency.

A unique three-dimensional shape of the protein.

Oil or butter.

Hydrophobic / Van der Waals interactions.

Polymerization of α-glucose.

Lecithin.

It is unique to each polypeptide chain.

Nucleic acids are macromolecules that store and transmit genetic information.

In fruits and vegetables.

A conjugated protein that contains a pigment, such as myoglobin or hemoglobin.

Long chains of monosaccharides connected by glycosidic bonds.

Hydrophilic head and hydrophobic tail.

The activation energy and the energy changes during a reaction.

The active site is not changed after binding with the substrate.

α-glucose has a specific arrangement of hydroxyl groups that distinguishes it from β-glucose.

Changes in pH can disrupt H & ionic bonds, affecting protein stability.

Adenine pairs with Thymine (A-T) and Cytosine pairs with Guanine (C-G).

Enzymes are proteins that catalyze biochemical reactions.

The enzyme is not changed or damaged and can be reused.

It acts as a base and can accept a proton.

They support growth.

The sequence of amino acids in a polypeptide chain.

C5H10O4.

A bond formed between two monosaccharides through a condensation reaction.

Lipids are used for energy storage, insulation, and making up cell membranes.

By being lighter and hydrophobic.

No, they are insoluble in water and form colloids.

Polymerization of β-glucose.

Benedict's test is used to identify reducing and non-reducing sugars.

Amino acids.

Dipeptides form when two amino acids join via a peptide bond, and polypeptides form when multiple amino acids are linked together.

Long chains of monosaccharide units linked together.

Triglycerides have three fatty acids, while phospholipids have two fatty acids and a phosphate group.

In fruits and honey.

A bond formed between two monosaccharides through a condensation reaction.

They are used to create a variety of polymers.

A specific site on the enzyme that binds to a specific substrate.

Carbohydrates formed by the combination of two monosaccharides.

The model suggesting that the enzyme's active site is a perfect fit for the substrate.

Starch or glycogen.

A site other than the active site where molecules can bind, influencing enzyme activity.

β-glucose has a different arrangement of hydroxyl groups compared to α-glucose.

They are water-repelling.

Relatively soluble, forming a colloid.

Hydrogen bonds.

They are lighter and hydrophobic, meaning they do not associate with water.

RNA transfers genetic information from DNA to ribosomes for protein synthesis.

A non-protein compound that is essential for the function of a conjugated protein.

Lysozyme.

Saturated fatty acids have no double bonds between carbon atoms, while unsaturated fatty acids have one or more double bonds.

Based on the number of carbon atoms and the position of functional groups.

Cholesterol.

Both DNA and RNA are nucleic acids made of nucleotides and play crucial roles in genetic information.

A process that breaks down polymers into monomers by adding water.

The formation of large molecules made up of repeating units of monomers.

A bond formed between monosaccharides during polymerization.

Starch or glycogen.

NH2 group.

DNA is composed of nucleotides, which include a phosphate group, a sugar, and a nitrogenous base.

By hydrolysis.

It accounts for the dynamic nature of enzyme-substrate interactions and the ability of enzymes to adapt to different substrates.

Glycogen.

The ability of the structure to stretch and return.

Peptide bonds, hydrogen bonds, disulfide bonds, ionic bonds, hydrogen bonds (between R groups), and hydrophobic (van der Waals) interactions.

More than twice the energy.

A monosaccharide with 3 carbon atoms.

Ribose and deoxyribose.

Enzymes, hormones, antibodies.

Alanine, arginine, asparagine.

It makes the head hydrophilic and gives the molecule acidic properties.

The folding or coiling of the polypeptide chain into alpha-helices or beta-sheets.

A monosaccharide with 6 carbon atoms.

Water is essential for biochemical reactions and maintaining cellular structure.

The minimum energy required for a chemical reaction to occur.

Within every 30 units.

A process that forms polymers by joining monomers and releasing water.

A glycosidic bond.

Water is a solvent for biochemical reactions and helps maintain cell structure.

Cellulose.

Unbranched, long straight chain.

Peptide bonds and hydrogen bonds (between C=O & NH group of backbone).

α-glucose molecules.

A long chain called a polypeptide.

Starch or glycogen.

A hydrolysis reaction is the process of breaking down polymers into monomers by adding water.

They are essential for protein structure and function.

Starch or glycogen.

It breaks down into two α-glucose molecules.

Nucleic acids store and transmit genetic information.

The Lock and Key model.

C5H10O5 for ribose and C5H10O4 for deoxyribose.

Triglycerides form through the condensation reaction between glycerol and three fatty acids, resulting in the release of water molecules.

They have a variety of functions essential for bodily processes.

Enzymes are proteins that catalyze biochemical reactions.

A conjugated protein that has a polysaccharide component.

They form a ring structure, which is more stable.

Two monosaccharides linked by a glycosidic bond.

Through hydrolysis, which involves the addition of water molecules.

α-glucose forms starch or glycogen, while β-glucose forms cellulose.

They are water-attracting.

C3H6O3.

Saturated fatty acids have no double bonds between carbon atoms, while unsaturated fatty acids have one or more double bonds.

Increased temperature can lead to denaturation by breaking bonds and interactions.

Large molecules made up of many sugar molecules; they are polymers.

Yes, the enzyme does not change and can be reused after the reaction.

Glucose.

Higher substrate concentration can increase the rate of reaction until saturation is reached.

The enzyme reverts to its original conformation when the product is released.

α - 1,4 glycosidic bond.

The Biuret test is used to detect the presence of proteins.

The overall three-dimensional shape formed by the folding of the polypeptide chain.

In adipose tissue.

Enzymes are proteins that catalyze biochemical reactions.

ATP (adenosine triphosphate) is the primary energy carrier in cells.

Nucleotides.

Ideal for energy storage (insoluble, coiled, compact).

A sugar with 6 carbon atoms.

The active site undergoes a conformational change to fit the substrate more effectively.

One or more polypeptide chains folded and coiled into a specific conformation.

Fats, steroids, and phospholipids.

It links amino acids together to form polypeptides.

A glycosidic bond is a type of covalent bond that links monosaccharides together to form disaccharides and polysaccharides.

An amino acid consists of a central carbon atom, an amino group, a carboxyl group, a hydrogen atom, and a variable R group (side chain).

Enzyme - Substrate Complex (ES).

A glycosidic bond.

Glucose, galactose, and fructose.

Triglycerides are primarily energy storage molecules, while phospholipids are key components of cell membranes, providing structure and function.

Blood sugar.

Starch or glycogen.

They act as padding for internal organs.

Water is a solvent for biochemical reactions and helps maintain cell structure.

Forming cell membranes.

Cellulose.

Fructose.

Fibrous and Globular.

Cellulose.

Keratin in hair, nails, and wool.

Proteins that function well when joined with a non-protein compound, known as a prosthetic group.

Carbohydrates serve as a primary energy source and structural components.

Carbon (C), Hydrogen (H), Oxygen (O), Nitrogen (N), and sometimes Sulfur (S).

Polysaccharides are not sweet.

Sucrose.

An RNA nucleotide consists of a phosphate group, a ribose sugar, and a nitrogenous base.

Cellulose.

C6H12O6.

They typically have a backbone of carbon atoms with hydroxyl groups and a carbonyl group.

Saturated fatty acids have no double bonds between carbon atoms, while unsaturated fatty acids have one or more double bonds.