AP Bio Unit 1

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26 Terms

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polarity

  • When there are differences in atomic electronegativities

  • Water is polar due to the oxygen being negative and the hydrogen being positive

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hydrogen bond

  • A weak bond interaction between the negative and positive regions of 2 separate molecules

  • Water molecules form hydrogen bonds with other water molecules

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cohesion

When 2 of the same molecules form hydrogen bonds with each other

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adhesion

When 2 different molecules form hydrogen bonds with each other

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surface tension

  • When many water molecules are bonded tightly together near the surface of the water

  • Helps plants floating on the water with photosynthesis

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solvency

When water molecules use adhesion to break apart other molecules

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high heat capacity

Water’s cohesive property allows it to absorb a lot of thermal energy before changing chemical states, resisting sudden changes in temperature

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capillary action

  • Water can go up a tube with its cohesive and adhesive abilities

  • Helps bring water up plant roots

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carbon

  • Used to build Carbohydrates, Lipids, Proteins, and Nucleic Acids

  • Stores energy

  • Builds basic cell structures

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nitrogen

Used to build proteins and nucleic acids

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phosphorous

Used to build certain lipids and nucleic acids

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monomers

  • Chemical subunits used to create polymers

  • Connect to other monomers through covalent bonds

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polymer

A macromolecule made of many monomers

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dehydration synthesis

  • OH and H come off of 2 monomers, joining the monomers together with a covalent bond

  • H2O is the byproduct

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hydrolysis

  • H2O splits apart a polymer

  • Opposite of dehydration synthesis

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nucleic acids

  • 3’ hydroxyl end and 5’ phosphate end

  • Antiparallel 5’-3’ direction

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adenine-thymine bond

  • Held together by 2 hydrogen bonds

  • Destabilizes faster than guanine-cytosine

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guanine-cytosine

  • Held together by 3 hydrogen bonds

  • Destabalizes slower than adenine-thymine

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amino acids

Held together by covalent bonds from dehydration synthesis

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primary structure of proteins

Determined by the sequence of amino acids held together by covalent bonds, called peptide bonds

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secondary structure of proteins

Arises through local folding of the amino acid chain into elements such as alpha-helices and beta-sheets

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tertiary structure of proteins

  • The overall 3D shape of the protein and often minimizes free energy

  • Various types of bonds and interactions stabilize the protein at this level

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quaternary structure of proteins

Arises from the interactions between multiple polypeptide units

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carbohydrates

Held together by covalent bonds from dehydration synthesis

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DNA

  • Double-stranded

  • Contains thymine

  • Deoxyribose sugar

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RNA

  • Single-stranded

  • Contains uracil

  • Ribose sugar