Biological Macromolecules Overview
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Questions and Answers

What is the primary structure of a protein?

  • The interactions among the side chains of amino acids
  • The sequence of amino acids in the protein (correct)
  • The 3-dimensional shape of the protein
  • The coils and folds in the polypeptide chain

Which of the following statements is true regarding protein structure?

  • The conformation of a protein determines how it functions (correct)
  • Secondary structure refers only to the primary amino acid sequence
  • The structure of a protein has no impact on its function
  • A protein with quaternary structure cannot have tertiary structure

What defines the tertiary structure of a protein?

  • The unique sequence of amino acids
  • Interactions among various side chains (R groups) (correct)
  • The presence of multiple polypeptide chains
  • The arrangement of coils and folds

Which level of protein structure involves coils and folds like α-helices and β-pleated sheets?

<p>Secondary structure (C)</p> Signup and view all the answers

What characterizes the quaternary structure of a protein?

<p>The combination of multiple polypeptide chains into a functional unit (A)</p> Signup and view all the answers

What is the primary function of chaperones in protein folding?

<p>To assist in the proper folding of other proteins (C)</p> Signup and view all the answers

In which cellular locations can chaperones be found?

<p>Cytosol, mitochondria, chloroplasts, and ER (D)</p> Signup and view all the answers

What happens to the cap of a chaperonin during the protein folding process?

<p>It changes shape to create a hydrophilic environment (D)</p> Signup and view all the answers

What is the correct order of actions performed by chaperonins during protein folding?

<p>Polypeptide enters, cap attaches, folded protein is released (C)</p> Signup and view all the answers

Which of the following best describes the secondary structure of proteins?

<p>Structures such as α helixes and β pleated sheets (C)</p> Signup and view all the answers

What technique is primarily used to determine a protein's three-dimensional structure?

<p>X-ray crystallography (A)</p> Signup and view all the answers

What type of mutation causes sickle-cell disease?

<p>Missense mutation (D)</p> Signup and view all the answers

How many polypeptides are present in a hemoglobin molecule?

<p>4 polypeptides (A)</p> Signup and view all the answers

What amino acid substitution occurs in the hemoglobin of individuals with sickle-cell disease?

<p>Glutamic acid to Valine (B)</p> Signup and view all the answers

What is the primary role of hemoglobin in the body?

<p>Carrying oxygen (D)</p> Signup and view all the answers

In the context of protein structure, what does X-ray diffraction reveal?

<p>The overall three-dimensional folding (B)</p> Signup and view all the answers

Which component of hemoglobin directly binds oxygen?

<p>Heme groups (C)</p> Signup and view all the answers

What impact does a single amino acid substitution have on proteins like hemoglobin?

<p>Can drastically alter protein function (B)</p> Signup and view all the answers

What is the general structure of a fatty acid?

<p>R-COOH (B)</p> Signup and view all the answers

Which of the following statements is true regarding saturated fatty acids?

<p>They are solid at room temperature. (A)</p> Signup and view all the answers

What distinguishes unsaturated fatty acids from saturated fatty acids?

<p>Unsaturated fatty acids have one or more double bonds. (A)</p> Signup and view all the answers

What is the typical carbon chain length for fatty acids mentioned?

<p>16-18 carbons (C)</p> Signup and view all the answers

Which of the following fatty acids is classified as saturated?

<p>Stearic acid (A)</p> Signup and view all the answers

What type of fats are made from unsaturated fatty acids?

<p>Unsaturated fats or oils (A)</p> Signup and view all the answers

Which of the following statements is true about the physical state of saturated and unsaturated fats?

<p>Saturated fats are solid while unsaturated fats are liquid. (A)</p> Signup and view all the answers

From which sources are unsaturated fatty acids primarily derived?

<p>Plants and fish (C)</p> Signup and view all the answers

What is the role of enzymes in biological processes?

<p>They speed up chemical reactions by acting as catalysts. (D)</p> Signup and view all the answers

Which of the following correctly describes a polypeptide?

<p>A polypeptide is a polymer made up of amino acids. (A)</p> Signup and view all the answers

Which function is NOT attributed to proteins?

<p>Energy production (C)</p> Signup and view all the answers

How do proteins contribute to cellular communications?

<p>By serving as receptors and signaling molecules. (B)</p> Signup and view all the answers

What is a characteristic of the sequence of amino acids in a polypeptide?

<p>It determines the protein's physical structure. (B)</p> Signup and view all the answers

Which statement about proteins is true?

<p>Proteins can be composed of one or more polypeptides. (A)</p> Signup and view all the answers

What percentage of the dry mass of most cells is made up of proteins?

<p>More than 50% (A)</p> Signup and view all the answers

Which function of proteins is related to the immune system?

<p>Defense against foreign substances (B)</p> Signup and view all the answers

What are the two primary forms of secondary structure in polypeptides?

<p>Alpha-helix and beta-pleated sheet (A)</p> Signup and view all the answers

Which structural feature is characteristic of the beta-pleated sheet?

<p>Parallel or antiparallel arrangements of polypeptide strands (D)</p> Signup and view all the answers

What kind of bonding primarily stabilizes the secondary structures of proteins?

<p>Hydrogen bonding (A)</p> Signup and view all the answers

In the context of secondary structure, what is the significance of the amino acid sequence?

<p>It dictates the pattern of hydrogen bonds. (B)</p> Signup and view all the answers

How would you describe the alpha-helix structure in proteins?

<p>A compact, tubular structure that coils (A)</p> Signup and view all the answers

Which of the following amino acid properties can influence secondary structure formation?

<p>Hydrophobicity and charge of side chains (C)</p> Signup and view all the answers

Which configuration of the beta-pleated sheet does NOT occur?

<p>Single-strand beta-pleated sheets (D)</p> Signup and view all the answers

What type of structure forms when a segment of a polypeptide chain coils into a repeated pattern?

<p>Secondary structure (D)</p> Signup and view all the answers

Flashcards

Fatty acid

A long chain of carbon atoms with a carboxyl group (COOH) at one end.

Saturated fatty acids

Fatty acids with no double bonds between carbon atoms. They have the maximum number of hydrogen atoms possible.

Unsaturated fatty acids

Fatty acids with one or more double bonds between carbon atoms.

Chain length of fatty acids

The number of carbon atoms in the chain.

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Degree of unsaturation in fatty acids

The number and positions of double bonds in the chain.

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Saturated fats

Fats composed mainly of saturated fatty acids, typically solid at room temperature.

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Unsaturated fats or oils

Fats composed mainly of unsaturated fatty acids, typically liquid at room temperature.

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Cis double bond in fatty acids

A type of unsaturated fatty acid with a specific configuration of the double bond, causing bending and altering the properties of the fatty acid.

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Primary Structure

The unique sequence of amino acids in a protein chain. Think of it like the alphabet letters that make up a word.

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Secondary Structure

The local folding patterns of the polypeptide chain. It involves alpha-helices (spiral shapes) and beta-pleated sheets (flattened, folded structures).

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Tertiary Structure

The overall three-dimensional shape of a protein determined by interactions between amino acid side chains (R-groups). Considered the functional form of the protein.

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Quaternary Structure

The structure formed when two or more polypeptide chains (subunits) come together to form a functional protein.

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Protein Conformation and Function

A protein's specific shape which defines its function. This shape is determined by the sequence of amino acids.

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Protein structure

The three-dimensional shape of a protein, which is determined by the sequence of amino acids in the polypeptide chain.

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Alpha-helix

A helical structure formed by hydrogen bonding between amino acids in a polypeptide chain.

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Beta-sheet

A sheet-like structure formed by hydrogen bonding between amino acids in different polypeptide chains.

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Protein folding

The specific arrangement of amino acids in a protein, which dictates the protein's function.

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Protein denaturation

A change in the three-dimensional structure of a protein, which can affect its function.

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What are proteins?

Proteins are large, complex molecules that perform a wide range of functions in living organisms.

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What are proteins made of?

Proteins are polymers made up of chains of amino acids linked together.

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What determines a protein's function?

The sequence of amino acids determines the shape of the protein, which is the primary factor in its function.

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What are some of the roles of proteins?

They provide structural support, store nutrients, transport substances, enable cell communication, facilitate movement, and defend against foreign substances.

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What are enzymes?

Enzymes are proteins that act as catalysts to speed up chemical reactions in living organisms.

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How do enzymes work?

Enzymes have a specific active site that binds to a specific substrate molecule.

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What is a polypeptide?

Proteins consist of one or more polypeptide chains, which are long chains of amino acids linked together by peptide bonds.

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How does the sequence of amino acids affect the structure of a protein?

The sequence of amino acids in a polypeptide determines its three-dimensional structure, which is crucial for its function.

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Chaperones

These are protein structures that help other proteins fold correctly. They can be found in different parts of the cell like the cytosol, mitochondria, chloroplasts, and the endoplasmic reticulum (ER).

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Chaperonins

A type of chaperone protein that acts as a cylindrical structure to help fold other proteins within a hydrophilic environment. It consists of a cap that attaches to the cylinder to trigger a shape change to create a suitable environment for folding.

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Step 1 of Chaperonin Action

An unfolded polypeptide chain enters the cylinder of the chaperonin.

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Step 2 of Chaperonin Action

The cap attaches to the chaperonin cylinder, causing it to change shape and create a hydrophilic environment for the polypeptide to fold.

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X-ray Crystallography

A technique used to determine the 3-dimensional structure of a protein by analyzing how X-rays are diffracted by the protein crystals.

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X-ray Diffraction Pattern

A pattern produced when X-rays pass through a protein crystal. This pattern provides information about the arrangement of atoms within the protein.

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Sickle-Cell Disease

A genetic disorder that affects the shape of red blood cells. It results from a single amino acid substitution in the protein haemoglobin.

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Haemoglobin

A globular protein responsible for carrying oxygen in the blood. It consists of four polypeptide chains: two alpha and two beta chains.

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Heme

A molecule that binds to haemoglobin and contains an iron atom. This iron atom is essential for oxygen binding.

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Glu → Val Mutation

The substitution of a glutamic acid (Glu) with a valine (Val) amino acid in the beta chain of haemoglobin. This mutation leads to sickle-cell disease.

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Impact of Single Amino Acid Substitution

A single amino acid change can have a significant impact on the protein's structure and function. This demonstrates the importance of specific amino acid sequence in protein folding.

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Study Notes

Macromolecules

  • Macromolecules are large molecules with complex structures
  • They are composed of thousands of covalently connected atoms
  • Small organic molecules are joined together to form larger molecules within cells
  • All living organisms are made up of 4 classes of biological macromolecules: carbohydrates, lipids, proteins, and nucleic acids
  • Molecular structure and function of macromolecules are closely related

4 Major Categories of Biological Macromolecules

  • Carbohydrates
  • Lipids
  • Proteins
  • Nucleic acids

Carbohydrates

  • Carbohydrates serve as fuel and building material
  • Carbohydrates are composed of carbon, hydrogen, and oxygen
  • The molecular formula is multiples of the unit (CH₂O)ₙ
  • Examples include pentoses (C₅H₁₀O₅) like ribose and deoxyribose, and hexoses (C₆H₁₂O₆) like glucose and fructose.
  • Biologically important carbohydrates are also called sugars
  • Monosaccharides are the simplest carbohydrates, single sugars (monomers)
  • Polysaccharides are carbohydrate polymers composed of many sugar building blocks
  • There are four categories of carbohydrates:
    • Monosaccharides (e.g., glucose, fructose)
    • Disaccharides (e.g., maltose, sucrose, lactose)
    • Oligosaccharides (composed of 20–30 monosaccharides)
    • Polysaccharides (e.g., starch, glycogen, cellulose, chitin)
  • Monosaccharides serve as fuel for cells and raw materials for building molecules
  • Monosaccharides are classified by:
    • The location of the carbonyl group (as aldose or ketose)
    • The number of carbons in the carbon skeleton
  • Monosaccharides can be linear but in aqueous solutions many form rings
  • A disaccharide is formed when a dehydration reaction joins two monosaccharides; this covalent bond is called a glycosidic linkage. Common examples include maltose (glucose + glucose), lactose (glucose + galactose), and sucrose (glucose + fructose).
  • Polysaccharides include storage polysaccharides (starch and glycogen) and structural polysaccharides (cellulose and chitin).
    • Starch, the major storage polysaccharide in plants, consists of amylose (20-30%) and amylopectin (70-80%).
    • Glycogen, the storage polysaccharide in animals, is highly branched and functions to store glucose.
    • Cellulose, a structural polysaccharide in plant cell walls, is a glucose polymer with different glycosidic linkages from starch. Cellulose is difficult to digest for humans.
    • Chitin, a structural polysaccharide in fungal cell walls and arthropod exoskeletons, is similar in structure to cellulose but contains nitrogen.

Lipids

  • Lipids are hydrophobic - they do not mix with water
  • Lipids are a diverse group of hydrophobic molecules that do not consist of polymers
  • Biologically important lipids: fats, phospholipids, steroids
    • Fats are triglycerides: glycerol + 3 fatty acids (important energy source)
    • Phospholipids have a glycerol backbone, two fatty acid "tails", and a phosphate group "head". Phospholipids are amphipathic (hydrophilic head and hydrophobic tails)
    • Steroids have four fused carbon rings (e.g., cholesterol, hormones). Cholesterol is important for cell membranes in animals.

Proteins

  • Proteins have many structures, thus a wide range of functions
  • Proteins account for more than 50% of the dry mass of most cells
  • Protein functions include structural support, storage, transport, cellular communication, movement, and defense against foreign substances)
  • Proteins are polymers of amino acids
  • Polypeptides range in length from a few to more than a thousand monomers
  • Amino acids have carboxyl and amino groups that differ in properties due to differing R-groups
  • The 20 amino acids are categorized as nonpolar, polar, or electrically charged.
  • Proteins have four levels of structure:
    • Primary structure: the unique sequence of amino acids forming a polypeptide chain
    • Secondary structure: coils and folds in the polypeptide chain (e.g., α-helices and β-pleated sheets)
    • Tertiary structure: the 3D structure of the polypeptide chain determined by interactions among various side chains (R groups)
    • Quaternary structure: results when a protein consists of multiple polypeptide chains (subunits)
  • Enzymes are specific types of proteins that act as catalysts, speeding up chemical reactions
  • Protein conformation depends on physical and chemical conditions of the protein's environment
  • Denaturation is the loss of a protein's native conformation due to the unraveling of the protein, causing it to lose its function. Denaturation can result from pH changes, salt concentration changes, temperature changes, and other environmental factors.

Nucleic Acids

  • Nucleic acids store and transmit hereditary information
  • The amino acid sequence of a polypeptide is encoded by a unit of inheritance called a gene. Genes are made of DNA. DNA is a nucleic acid.
  • DNA stores information for protein synthesis.
  • DNA directs RNA synthesis.
  • DNA directs protein synthesis through mRNA (messenger RNA)
  • Nucleic acids exist as polymers called polynucleotides
  • Each polynucleotide consists of monomers called nucleotides
  • A nucleotide = nitrogenous base + pentose sugar + phosphate group
  • There are two types of nucleic acids: DNA and RNA.
  • DNA is double-stranded while RNA is single-stranded.
  • The sequence of bases along a nucleotide polymer is unique for each gene and specifies the amino acid sequence of a protein.
  • DNA replication is the copying of all DNA molecules into a second set, required before cell division.

Protein-Folding & Chaperones

  • Most proteins fold into a specific 3D structure to become fully functional.
  • Chaperones are proteins that help other proteins fold correctly, assist as needed.
  • Chaperones locate in cytosol, mitochondria, chloroplasts, and ER.

Protein Structure Determination

  • X-ray crystallography is used to determine a protein's three-dimensional structure.

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Explore the fascinating world of biological macromolecules in this quiz. Learn about the four major categories: carbohydrates, lipids, proteins, and nucleic acids, and their structures and functions. Understand how these molecules are essential to all living organisms.

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