AP Biology Unit 1: The Chemistry of Life

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Questions and Answers

Which of the following macromolecules serves primarily as structural support in plant cells?

  • Cellulose (correct)
  • Glycogen
  • Starch
  • Chitin

What is the bond type called that forms between two monosaccharides to create a disaccharide?

  • Glycosidic linkage (correct)
  • Ionic bond
  • Peptide bond
  • Hydrogen bond

Which of these carbohydrates is primarily used for energy storage in animals?

  • Cellulose
  • Fructose
  • Sucrose
  • Glycogen (correct)

Which carbohydrate has a 1,4 beta linkage, making it indigestible to humans?

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

Which of the following correctly describes the composition of carbohydrates?

<p>Composed of carbon, hydrogen, and oxygen in a 1:2:1 ratio (C)</p> Signup and view all the answers

What type of bond primarily stabilizes the alpha helix and beta pleated sheet structures in proteins?

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

Which of the following characteristics contributes to the tertiary structure of proteins?

<p>Interactions between R groups (B)</p> Signup and view all the answers

What is a common characteristic of hydrophobic R groups in amino acids?

<p>They contain primarily carbon and hydrogen. (D)</p> Signup and view all the answers

Which of the following statements correctly describes the quaternary structure of a protein?

<p>It can consist of multiple polypeptide chains coming together. (C)</p> Signup and view all the answers

Which component of nucleic acids is responsible for their overall negative charge?

<p>Phosphate groups in nucleotides (C)</p> Signup and view all the answers

What is the primary structure of proteins composed of?

<p>A long string of amino acids (D)</p> Signup and view all the answers

What type of bond forms between adjacent amino acids?

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

Which statement about the R group of amino acids is true?

<p>It determines the functional properties of the amino acid. (D)</p> Signup and view all the answers

What type of bond is involved in the stabilization of protein tertiary structure?

<p>All of the above (D)</p> Signup and view all the answers

What are the two functional groups present in all amino acids?

<p>Carboxylic acid and Amine group (B)</p> Signup and view all the answers

What is the difference between the sugar found in DNA and RNA?

<p>RNA contains ribose while DNA contains deoxyribose. (B)</p> Signup and view all the answers

Which pair of nitrogenous bases is correctly matched with the number of hydrogen bonds they form?

<p>Adenine and Thymine - two bonds (D)</p> Signup and view all the answers

What characteristic distinguishes purines from pyrimidines?

<p>Purines include Adenine and Guanine; pyrimidines include Cytosine and Thymine. (A)</p> Signup and view all the answers

Which statement correctly describes the orientation of DNA strands?

<p>One strand runs from 5' to 3' while the other runs from 3' to 5'. (B)</p> Signup and view all the answers

Which of the following is true regarding the structure of lipids?

<p>Lipids are primarily made up of carbon, hydrogen, and often oxygen. (A)</p> Signup and view all the answers

Flashcards

Monosaccharide

A carbohydrate monomer (simple sugar) that serves as a primary energy source in cells. Examples include glucose, fructose, and galactose.

Polysaccharide

A carbohydrate polymer made up of many monosaccharides linked together. Examples include starch, glycogen, cellulose, and chitin.

Glycosidic Linkage

The bond that connects monosaccharides together to form disaccharides and polysaccharides.

Starch

A storage polysaccharide found in plants. It's the energy reserve in potatoes, grains, and other plant foods.

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Cellulose

A structural polysaccharide found in plant cell walls. It provides rigidity and support to plants, making them stand tall.

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Peptide Bond

The type of chemical bond formed between the carboxyl group of one amino acid and the amino group of the next amino acid, creating a chain of amino acids.

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Primary Structure

The linear sequence of amino acids in a protein, forming the basic building block of a protein.

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Secondary Structure

The folding of the primary structure into alpha-helices or beta-pleated sheets, stabilized by hydrogen bonds.

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Tertiary Structure

The three-dimensional shape of a protein determined by interactions between R-groups of amino acids.

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Quaternary Structure

The structure formed when multiple polypeptide chains interact, forming a complex protein.

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DNA (Deoxyribonucleic Acid)

A type of nucleic acid that stores and transmits genetic information. It consists of two long chains of nucleotides linked by hydrogen bonds. Each nucleotide is composed of a deoxyribose sugar, a phosphate group, and one of four nitrogenous bases: adenine (A), cytosine (C), guanine (G), and thymine (T).

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RNA (Ribonucleic Acid)

A type of nucleic acid involved in protein synthesis. It consists of a single chain of nucleotides linked by phosphodiester bonds. Each nucleotide is composed of a ribose sugar, a phosphate group, and one of four nitrogenous bases: adenine (A), cytosine (C), guanine (G), and uracil (U).

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Thymine (T)

A type of nucleotide base that is found in DNA but not in RNA. It pairs with Adenine through two hydrogen bonds.

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Phosphodiester Linkage

The bond that links nucleotides together in a nucleic acid chain. It involves the phosphate group of one nucleotide and the hydroxyl group of the sugar on the adjacent nucleotide.

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What is the primary structure of a protein?

The primary structure of a protein is the linear sequence of amino acids linked together by peptide bonds.

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What are the secondary structures of a protein?

The secondary structure of a protein refers to the local folding patterns of the polypeptide chain, primarily due to hydrogen bonding between backbone atoms. Two common secondary structures are the alpha-helix (a spiral shape) and the beta-pleated sheet (a folded sheet-like structure).

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What is the tertiary structure of a protein?

The tertiary structure of a protein describes the overall three-dimensional shape of a single polypeptide chain. It's determined by interactions between the R groups of amino acids, including hydrogen bonding, hydrophobic interactions, ionic bonding, and disulfide bridges.

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What is the quaternary structure of a protein?

The quaternary structure of a protein refers to the arrangement of multiple polypeptide chains (subunits) that come together to form a functional protein. Not all proteins have a quaternary structure.

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What are the three types of R-groups and how do they affect protein folding?

The R-groups of amino acids can be hydrophilic (polar, water-loving), hydrophobic (non-polar, water-fearing), or charged (positive or negative). These characteristics greatly influence how a protein folds and interacts with its environment.

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Study Notes

Macromolecules

  • Four macromolecules (carbohydrates, proteins, nucleic acids, lipids) are crucial for biological processes.
  • Each has a unique structure and function.

Carbohydrates

  • Composed of carbon, hydrogen, and oxygen (1:2:1 ratio).
  • Monomer: monosaccharide (e.g., glucose, fructose, galactose).
  • Polymer: polysaccharide.
  • Glucose structure: ring structure; chemical formula C6H12O6.
  • Dehydration reaction joins two monosaccharides to form a disaccharide (e.g., sucrose, lactose, maltose).
  • Bond between monosaccharides: glycosidic linkage.
  • Polysaccharides: cellulose (plant cell walls, structural), chitin (fungi cell walls, exoskeletons), starch (plant energy storage), glycogen (animal energy storage).
  • Starch and cellulose differ in glycosidic linkage (alpha-1,4 for starch; beta-1,4 for cellulose) - allowing us to break one but not the other.
  • Symbiotic relationships exist (termite gut microbes breaking down cellulose).

Proteins

  • Composed of carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur.
  • Monomer: amino acid.
  • Amino acid structure: central carbon bonded to an amino group (NH2), a carboxyl group (COOH), a hydrogen atom, and a variable R group.
  • Peptide bond forms between the carboxyl group of one amino acid and the amino group of the next.
  • Directionality: N-terminus (amino end) to C-terminus (carboxyl end).
  • Protein structure levels:
    • Primary: linear sequence of amino acids.
    • Secondary: alpha helix or beta-pleated sheet (hydrogen bonds in the protein backbone).
    • Tertiary: 3D structure formed by various bonds (covalent, ionic, hydrogen, van der Waals, hydrophobic interactions) between R groups.
    • Quaternary: multiple polypeptides forming a larger protein (e.g., collagen, hemoglobin).
  • R groups can be hydrophobic, hydrophilic, or charged.
  • Hydrophobic R groups fold inward, while hydrophilic ones fold outwards.
    • Charged ones can form ionic bonds with water or other polar molecules.

Nucleic Acids

  • Composed of carbon, hydrogen, oxygen, nitrogen, and phosphorus (in phosphate groups).
  • Monomer: nucleotide.
  • Nucleotide structure: phosphate group, nitrogenous base (adenine, guanine, cytosine, thymine/uracil), and a pentose sugar (deoxyribose/ribose).
  • Phosphodiester linkage joins nucleotides.
  • Directionality: 5' end (phosphate) to 3' end (hydroxyl).
  • DNA structure: double helix; antiparallel strands; base pairing (A-T with two hydrogen bonds; C-G with three hydrogen bonds).
  • RNA structure: single-stranded; contains uracil instead of thymine.
  • Differences between DNA and RNA: sugar type (deoxyribose vs. ribose) and strandedness.

Lipids

  • Composed of carbon, hydrogen, and oxygen.
  • Non-polar.
  • Not polymers (no repeating monomer units).
  • Types:
    • Fats (triglycerides): glycerol backbone + 3 fatty acids linked by ester bonds.
      • Saturated fats (all single bonds) are solid at room temperature.
      • Unsaturated fats (at least one double bond) are liquid at room temperature (oils).
    • Phospholipids: glycerol backbone + 2 fatty acids + phosphate group.
      • Amphipathic (polar head, non-polar tails).
      • Form bilayers in water.
    • Steroids: four fused carbon rings (e.g., cholesterol, hormones). Key roles in cell signaling.

Water Properties

  • Polar covalent bonds (unequal electron sharing).
  • Hydrogen bonds between water molecules.
  • Cohesion: water molecules attracted to each other.
  • Adhesion: water molecules attracted to other polar substances.
  • Capillary action: combined effect of cohesion and adhesion.
  • Surface tension: resistance to increase in surface area due to hydrogen bonds.
  • Water is a universal solvent.
  • High specific heat: resists changes in temperature.
  • Ice is less dense than liquid water (hydrogen bonds stabilize crystal structure).
  • Evaporative cooling: heat absorbed to change water from liquid to gas phase.
  • pH: negative logarithm of hydrogen ion concentration (inverse relationship); pH scale (acidic/basic), significant for biological systems.

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