Macromolecules: Building Blocks of Life

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Questions and Answers

Which characteristic is common to proteins, carbohydrates, and lipids?

  • They all are macromolecules essential to living organisms. (correct)
  • They all contain nitrogen in their molecular structure.
  • They are all polymers formed through covalent bonding.
  • They are all constructed from amino acid monomers.

What determines the specific chemical properties that a functional group confers to a molecule?

  • The size of the molecule to which it is attached.
  • The presence of water molecules surrounding the molecule.
  • The specific arrangement and types of atoms in the functional group. (correct)
  • The number of carbon atoms in the molecule.

Which of the following is an example of a reaction that builds polymers from monomers?

  • Hydrolysis
  • Condensation (correct)
  • Oxidation
  • Reduction

What is the primary structural difference between a protein consisting of one polypeptide chain versus one with multiple polypeptide chains?

<p>The presence of a quaternary structure. (B)</p> Signup and view all the answers

Which type of bond is directly involved in the primary structure of a protein?

<p>Peptide bond (C)</p> Signup and view all the answers

How do amino acid side chains (R groups) contribute to the overall structure and function of a protein?

<p>By providing functional groups that determine the 3D structure and function. (D)</p> Signup and view all the answers

Which of the following best describes the properties of amino acids at the pH levels typically found in cells?

<p>Both the carboxyl and amino groups are ionized. (D)</p> Signup and view all the answers

Which statement correctly describes how a protein achieves its functional shape?

<p>A protein's shape is determined by its amino acid sequence and stabilized by various chemical interactions. (D)</p> Signup and view all the answers

Why is the sequence of amino acids critical to protein function?

<p>The sequence dictates the folding and thus the 3D shape of the protein. (C)</p> Signup and view all the answers

Which of the following is most likely to cause a protein to denature?

<p>Slowly and moderately increasing the temperature. (B)</p> Signup and view all the answers

What biological process involves breaking down polymers into monomers?

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

What property characterizes lipids, distinguishing them from proteins and carbohydrates?

<p>Their insolubility in water due to many nonpolar covalent bonds. (B)</p> Signup and view all the answers

Which functional group is commonly found in alcohols and enables them to form hydrogen bonds with water?

<p>Hydroxyl (B)</p> Signup and view all the answers

In what way do amino acids show both acidic and basic properties?

<p>They have both carboxyl and amino groups that can ionize. (A)</p> Signup and view all the answers

Which of the following is the most inclusive level of protein structure?

<p>Quaternary structure (A)</p> Signup and view all the answers

How does the shape of a protein relate to it's function?

<p>A protein's shape allows it to bind specific molecules or undergo chemical reaction. (A)</p> Signup and view all the answers

What class of compounds has the general formula $C_n(H_2O)_m$?

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

What type of bond is formed when monosaccharides are linked together to form disaccharides?

<p>Glycosidic bond (D)</p> Signup and view all the answers

What is the primary function of carbohydrates in biological systems?

<p>To store and transport energy. (D)</p> Signup and view all the answers

Which property distinguishes lipids from other macromolecules?

<p>They are largely hydrophobic. (A)</p> Signup and view all the answers

What role do phospholipids play in living organisms?

<p>Structural roles in cell membranes. (C)</p> Signup and view all the answers

Which of the following is a function of steroids?

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

What type of bond is formed when a hydroxyl group of glycerol reacts with the carboxyl group of fatty acid?

<p>Ester linkage (B)</p> Signup and view all the answers

What is the key structural difference between saturated and unsaturated fatty acids?

<p>Unsaturated fats contain one or more double bonds between carbon atoms. (A)</p> Signup and view all the answers

What property of phospholipids allows them to form bilayers in aqueous environments?

<p>They are amphipathic. (A)</p> Signup and view all the answers

Which of the following is a function of motor proteins?

<p>Cause movement of structures in the cell. (D)</p> Signup and view all the answers

Which of the following is a storage protein?

<p>Storage proteins (D)</p> Signup and view all the answers

What is an oligopeptide?

<p>A short polymer of less than 20 amino acids. (A)</p> Signup and view all the answers

Which of the following is an example of a denatured protein?

<p>A non-functional protein with broken hydrogen bonds. (C)</p> Signup and view all the answers

What is the purpose of defensive proteins?

<p>To recognize and respond to nonself substances, like antibodies. (A)</p> Signup and view all the answers

Which of these is part of the role of transport proteins?

<p>To bind and carry substance within the organism. (A)</p> Signup and view all the answers

What causes the formation of a disulfide bridge?

<p>Giving up H, two -SH groups can react to form a disulfide bridge. (C)</p> Signup and view all the answers

What aspect of protein structure is stabilized by hydrogen bonds?

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

Which of the following are components of lipids?

<p>fatty acids and glycerol (C)</p> Signup and view all the answers

What roles do carotenoids and chlorophylls play in a plant?

<p>Capture energy (A)</p> Signup and view all the answers

What is the main component of plant cell walls?

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

Why are lipids hydrophobic?

<p>The presence of hydrocarbons. (B)</p> Signup and view all the answers

What is the effect of high temperature on the hydrogen bonds and hydrophobic interactions of a protein?

<p>They break. (C)</p> Signup and view all the answers

Two molecules with the same chemical formula but different structures are called what?

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

Which chemical group is very reactive and important in energy-releasing reactions?

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

Which of the following is a polar group that is important in carbohydrates and in energy reactions?

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

Which functional group is charged, acidic, and enters into condensation reactions by giving up -OH.

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

If a protein's native conformation is disrupted due to environmental changes, which level of protein structure is the least likely to be affected?

<p>Primary structure (A)</p> Signup and view all the answers

How does the formation of a disulfide bridge contribute to the stabilization of a protein's structure?

<p>By forming a covalent bond between the R groups of two cysteine amino acids. (C)</p> Signup and view all the answers

Which of the following explains why lipids are not considered polymers in the same way as proteins and carbohydrates?

<p>Lipids do not consist of repeating monomer units linked by covalent bonds. (C)</p> Signup and view all the answers

If a researcher discovers a new type of linkage between monosaccharides in a polysaccharide, what kind of reaction is most likely involved in forming this linkage?

<p>Condensation reaction (A)</p> Signup and view all the answers

How would a significant increase in temperature likely affect the structure and function of a protein?

<p>It would disrupt the hydrogen bonds and hydrophobic interactions, leading to denaturation. (B)</p> Signup and view all the answers

If a certain biological molecule is found to be primarily hydrophobic and insoluble in water, and is composed of a glycerol molecule bonded to three long hydrocarbon chains, how would this molecule be classified?

<p>A lipid, specifically a triglyceride (C)</p> Signup and view all the answers

Considering the properties of amino acid R-groups, how would the distribution of polar and nonpolar amino acids likely influence the folding of a soluble protein in an aqueous cellular environment?

<p>Polar amino acids would be found primarily on the protein's surface, interacting with water. (D)</p> Signup and view all the answers

Why are carbohydrates important for energy storage?

<p>They can be quickly broken down into usable forms of energy by organisms. (A)</p> Signup and view all the answers

How do phospholipids play significant structural roles in cell membranes due to their amphipathic properties?

<p>They can form a bilayer with the hydrophobic tails facing inward and hydrophilic heads facing outward, creating a barrier to the movement of polar substances. (A)</p> Signup and view all the answers

What is the primary structural feature that distinguishes saturated fatty acids from unsaturated fatty acids?

<p>Unsaturated fatty acids contain one or more double bonds between carbon molecules, while saturated fatty acids do not. (C)</p> Signup and view all the answers

What is the role of carboxyl functional groups in condensation reactions involving amino acids?

<p>They donate -OH to form water. (B)</p> Signup and view all the answers

How do the chemical properties of the R groups affect the overall structure of a protein?

<p>The R groups can form hydrogen bonds, ionic bonds, or hydrophobic interactions, which help the protein fold into its appropriate shape. (D)</p> Signup and view all the answers

If a protein is composed of multiple polypeptide chains, what name is given to the overall structure?

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

Why do lipids have the property of being hydrophobic?

<p>They are composed predominantly of nonpolar bonds. (A)</p> Signup and view all the answers

What is the process by which monomers are combined to form a polymer?

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

The general formula for carbohydrates is $C_n(H_2O)_m$. What does this indicate about the composition of carbohydrates?

<p>A fixed ratio of carbon, hydrogen, and oxygen. (A)</p> Signup and view all the answers

What functional group is commonly found in alcohols?

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

Which property distinguishes lipids from proteins and carbohydrates?

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

What is the primary role of defensive proteins in living organisms?

<p>To recognize and respond to nonself substances. (A)</p> Signup and view all the answers

How do changes in pH affect protein structure?

<p>They alter the ionization patterns of exposed carboxyl and amino groups in the R groups of amino acids. (C)</p> Signup and view all the answers

Flashcards

Four kinds of molecules

Molecules characteristic of living things. Includes proteins, carbohydrates, lipids and nucleic acids.

Functional groups

Small groups of atoms that confer specific chemical properties when attached to a larger molecule.

Condensation reaction

A chemical reaction that produces water and forms macromolecules.

Hydrolysis

A chemical reaction that consumes water to break down macromolecules.

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Proteins

Polymers made of 20 amino acids in different proportions and sequences, consist of one or more polypeptide chains.

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Polypeptide chains

Unbranched, linear polymers of covalently bonded amino acids.

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Isomers

Molecules with the same chemical formula but atoms arranged differently.

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Primary structure (proteins)

The sequence of amino acids joined by peptide bonds.

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Secondary structure (proteins)

The polypeptide chains that may form α helices or β pleated sheets.

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Tertiary structure (proteins)

The definitive 3D shape of a protein.

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Quaternary structure (proteins)

Results from the ways in which subunits bind together and interact.

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Denatured protein

When protein is heated slowly and moderately, weak interactions disrupt. Secondary and tertiary structures break down.

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Native protein

A protein's normal and functional state.

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Carbohydrates

General formula: Cn(H2O)m. Act as source of stored energy, and as carbon skeletons.

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Monosaccharides

Simple sugars. Monomer.

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Disaccharides

Two monosaccharides linked by a covalent bond.

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Oligosaccharides

Several (3-20) monosaccharides.

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Polysaccharides

Made up of hundreds-thousands of monosaccharides.

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Glycosidic bonds

A bond between two monosaccharides.

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Starch

Principal energy storage compound of plants

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Cellulose

Main component of plant cell walls.

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Glycogen

Principal energy storage compound of animals

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Lipids

Hydrocarbons that are insoluble because of their many nonpolar covalent bonds.

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Hydrophobic

Aggregate together, away from water.

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Fats

Store energy; triglycerides, or simple lipids. Solid at room temperature.

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Oils

Store energy; triglycerides, or simple lipids. Liquid at room temperature.

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Triglycerides

The three fatty acids acids combined with each hydroxyl (-OH) group bonds to the carboxyl group (-COOH) of a fatty acid through covalent bonds.

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Amphipathic

Lipids with important components: part hydrophilic and part hydrophobic.

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Phospholipids

Play important structural roles in cell membranes. e.g., phosphatidylcholine.

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Saturated

No double bonds.

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Unsaturated

One or more double bonds

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Study Notes

Today's Objectives

  • Identify macromolecules characterizing living things
  • Learn functional groups giving macromolecules chemical properties
  • Understand the different amino acids comprising proteins and how protein structure gets determined
  • Introduction to the relationship between protein structure and function is provided
  • Understand the relationship between carbohydrate monomers and polymers, including examples
  • Components of lipids are described, including the biological roles of lipids

Molecules of Living Things

  • Proteins, carbohydrates, lipids, and nucleic acids characterize living things
  • Proteins are formed from different combinations of 20 amino acids
  • Carbohydrates are formed by linking together monosaccharides
  • Nucleic acids are formed from four kinds of nucleotides
  • Polymers are constructed by covalent bonding of smaller molecules called monomers

Functional Groups

  • Specific groups of atoms, called functional groups, occur frequently in biological molecules
  • Functional groups confer specific chemical properties when attached to a larger molecule

Protein Composition and Structure

  • Proteins are polymers made up of 20 amino acids in different proportions and sequences
  • The size of proteins ranges from small, like insulin with 51 amino acids, to huge, like titin with 24,000-36,000 amino acids
  • Proteins consist of one or more polypeptide chains
  • Polypeptide chains are unbranched (linear) polymers of covalently bonded amino acids
  • Each chain folds into a particular 3D shape

Amino Acids as Isomers

  • Amino acids can exist as optical isomers: D (dextro, right) and L (levo, left)
  • Only L-amino acids are found in proteins of most organisms
  • Isomers have the same chemical formula but are arranged differently

Amino and Carboxyl Groups

  • At the pH levels found in cells (usually pH 7.0–7.4), the carboxyl and amino groups of amino acids are ionized

R Groups

  • The side chains (or R groups) have functional groups
  • The functional groups are important in determining the 3D structure and function of a protein

Electrically Charged Amino Acids

  • Five amino acids have electrically charged side chains at pH levels typical of living cells
  • The side chains attract water (hydrophilic)
  • The side chains attract oppositely charged ions

Electrically Charged Amino Acids Examples

  • Arginine, histidine, and lysine have a +1 charge.
  • Aspartic acid and glutamic acid have a -1 charge.

Amino Acids with Polar Side Chains

  • Five amino acids have polar (δ+ and δ-) side chains
  • The polar side chains attract water (hydrophilic)
  • The polar side chains form hydrogen bonds with water and other polar substances
  • Serine, threonine, asparagine, glutamine, and tyrosine are examples of amino acids with polar side chains

Amino Acids with Nonpolar Side Chains

  • Seven amino acids have nonpolar hydrocarbon side chains
  • The side chains are hydrophobic
  • The hydrophobic side chains cluster together in aqueous solution
  • Alanine, isoleucine, leucine, methionine, phenylalanine, tryptophan, and valine are examples of amino acids with nonpolar side chains

Special Case Amino Acids

  • Three amino acids are special cases: cysteine, glycine, and proline

Cysteine

  • Cysteine has an -SH group
  • Cysteine can react with another cysteine side chain in an oxidation reaction to form a covalent bond
  • Forms a disulfide bridge

Glycine

  • Features a side chain equal to a single H atom
  • Glycine is small enough to fit into tight corners of interior of protein
  • Allows the protein to be flexible at its location
  • Glycine is generally hydrophobic

Proline

  • Has a modified amino group: it lacks an H atom and covalently bonds to a hydrocarbon side chain
  • The modified amino group creates a ring structure
  • Proline has limited capability of hydrogen bonding and rotation around the alpha carbon
  • Proline is found where a protein bends or loops

Primary Structure

  • Primary structure is formed by amino acids linked by peptide bonds, forming a polypeptide
  • Short polymers of <20 amino acids are called oligopeptides, or simply peptides

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