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  1. AP Biology
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What is polarity?

Unequal sharing of electrons creating a dipole moment in a molecule.

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What is polarity?

Unequal sharing of electrons creating a dipole moment in a molecule.

What are hydrogen bonds?

Weak intermolecular bonds between water molecules, crucial for water's properties.

What does hydrophilic mean?

Substances that are water-loving (polar) and dissolve easily in water.

What does hydrophobic mean?

Substances that are water-fearing (nonpolar) and do not mix with water.

Define dehydration synthesis.

Building polymers by removing water; monomers join, releasing a water molecule.

Define hydrolysis.

Breaking polymers by adding water; a water molecule breaks the bond between monomers.

What is a monomer?

A small subunit that can join with other similar molecules to form a polymer.

What is a polymer?

A large molecule (macromolecule) made of many monomers bonded together.

What happens when a protein denatures?

The protein loses its shape and function due to changes in temperature, pH, etc.

What is the effect of water's high specific heat?

It helps regulate temperatures in organisms and environments.

What is the effect of water's evaporative cooling?

As water evaporates, it takes heat with it, cooling the surface.

What causes water's polarity?

Unequal sharing of electrons between oxygen and hydrogen atoms.

What is the effect of hydrogen bonds in water?

Cohesion, adhesion, surface tension, and high specific heat.

What happens when hydrophobic substances are mixed with water?

They do not mix; they tend to aggregate or separate from the water.

What are the steps of dehydration synthesis?

  1. Monomers are positioned to form a bond. 2. A water molecule is removed. 3. A covalent bond forms between the monomers.

What are the steps of hydrolysis?

  1. A water molecule is added to the polymer. 2. The bond between two monomers is broken. 3. Two separate monomers are formed.

What are the levels of protein structure?

  1. Primary: Sequence of amino acids. 2. Secondary: Local folding (alpha-helices and beta-sheets). 3. Tertiary: 3D shape due to R-group interactions. 4. Quaternary: Multiple polypeptide chains bonded together.