Chapter 2 - Chemistry Comes Alive

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Last updated 1:39 AM on 10/8/26
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76 Terms

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Inorganic Compounds

  • Do not contain carbon

  • Ex: Water, Salts, Many acids and bases

  • CO2 and CO are exceptions to the rule


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Organic Compounds

  • Contains carbon

  • Ex: Carbohydrates, Lipids, Proteins, Nucleic acids


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properties of water

  • High heat capacity (Absorb and release heat)

  • High heat of vaporization (Water evaporation releases heat like sweating)

  • Polar molecule > universal solvent (Transport medium & Lubricant)

  • Reactivity (Important reactant in chemical reactions)

  • Cushion (protection)

*Most abundant inorganic compound (Accounts for 60%–80% of the volume of living cells)

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Hydrophilic substances

  • Polar molecules

  • Dissolve in water

  • Ex: Polar molecules, Ions, Small proteins


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Hydrophobic substances

  • Nonpolar molecules

  • Don’t dissolve in water

  • Have to be transported via carrier proteins

  • Ex: Nonpolar molecules & Metals


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Amphipathic molecules

  • Partially polar and nonpolar

  • > partially dissolves

  • Ex: Phospholipids & Glycolipids


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monomer

  • Single building block

  • Form polymers via dehydration synthesis reactions


<ul><li><p><span>Single building block</span></p></li><li><p style="text-align: left;"><span>Form polymers via dehydration synthesis reactions</span></p></li></ul><p></p>
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polymer

  • Chain of repeating monomers

  • Can be broken down into monomers via hydrolysis reactions


<ul><li><p><span>Chain of repeating monomers</span></p></li><li><p style="text-align: left;"><span>Can be broken down into monomers via hydrolysis reactions</span></p></li></ul><p></p>
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dehydration synthesis

monomers are joined by removal of OH from one monomer & removal of H from the other at the site of bond formation > anabolic

<p>monomers are joined by removal of OH from one monomer &amp; removal of H from the other at the site of bond formation &gt; anabolic</p>
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hydrolysis

monomers are released by the addition of a water molecule, adding OH to one monomer and H to the other

<p>monomers are released by the addition of a water molecule, adding OH to one monomer and H to the other</p>
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biological macromolecules always contain ?. may contain

always: C, H, O

may: N, P, S

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elements of carbohydrates

Rings of carbons, where the number of C is equal to the number of O. (CH2O)n

<p><span style="font-family: Helvetica, sans-serif;">Rings of carbons, where the number of C is equal to the number of O. (CH<sub>2</sub>O)<sub>n</sub></span></p>
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Molecular formula of carbohydrates

(CH2O)n

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function of carbohydrates

Fuel

Cell membrane structure (limited)

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are carbohydrates hydrophilic or hydrophobic?

hydrophilic

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types of carbohydrates

Monosaccharides

Disaccharides

Polysaccharides

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monomer of carbohydrates

monosaccharides (simple sugar)

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examples of carbohydrates

Glucose

Fructose

Galactose

Ribose

Deoxyribose

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two monosaccharides = ?. formed through ?

disaccharides; dehydration synthesis

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1.     Most prominent carbohydrate

2.     Main source of energy for most cells

3.     Can be stored in the liver and skeletal muscle as glycogen.

glucose

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Which monosaccharides combine to form sucrose

Glucose + Fructose

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Which monosaccharides combine to form lactose

Glucose + Galactose

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Which monosaccharides combine to form maltose

Glucose + Glucose

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polysaccharides

  • largest carbohydrate (made of many monosaccharide molecules)

  • >Combined via dehydration synthesis reactions.

  • low solubility (due to their size and branching)

  • most prominent example in humans: glycogen

  • other ex: Starch and cellulose (plants)


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Glycogen can be broken down into ? when blood glucose is low.

  • This is an example of ? feedback.

  • Stored in the ? & ?


glucose; negative feedback; liver and skeletal muscles.

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Glycogenesis

Storage of excess glucose in liver and skeletal muscle as glycogen

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Glycogenolysis

Liver hydrolyzes glycogen into glucose when needed

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Gluconeogenesis

Liver can make glucose from non-carbohydrate sources

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does Glycogenesis increase or decrease blood glucose?

Decreases

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does Glycogenolysis increase or decrease blood glucose?

Increases

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does Gluconeogenesis increase or decrease blood glucose?

Increases

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structure of lipids

C, H, O

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function of lipids

Insulation

Fuel

Cell structure

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are lipid molecules hydrophilic or hydrophobic?

hydrophobic

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types of lipids

Fatty acids

Triglycerides

Phospholipids

Steroids

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monomer of lipids

fatty acids

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structure of fatty acids

  • type of lipid

Carboxyl (COOH)

Hydrocarbon chain


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classes of fatty acids

Saturated fatty acids

Monounsaturated fatty acids

Polyunsaturated fatty acids

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Saturated fatty acids

  • No double bonds

  • solid @ room temp


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Monounsaturated fatty acids

  • 1 double bond

  • liquid @ room temp


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Polyunsaturated fatty acids

  • 2 or more double bonds

  • liquid @ room temp


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triglycerides structure

  • type of lipid

  • structure: 3 fatty acids + glycerol

  • Solids > fats

  • Liquid > oils


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triglycerides function

Energy storage and fuel (Lipogenesis and lipolysis)

Insulation

Protection

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lipogensis

3 fatty acids + glycerol → triglyceride + H₂O

  • Dehydration synthesis reaction


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lipolysis

triglyceride + H₂O → 3fatty acids + glycerol

  • Hydrolysis reaction


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phospholipids structure

  • type of lipid

  • modified triglyceride

  • Head (Polar)

>Phosphate-containing group

>Glycerol

  • Tail (Nonpolar)

>2 Fatty acids

  • amphipathic


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phospohlipids function

Cell membrane structure

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steroids structure

  • type of lipid

4 fused carbon rings

Composed of fatty acids


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functions of steroids

Cell membrane structure

Hormone synthesis

Bile synthesis

Vitamin D

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cholesterol

a.     Component of cell membranes

b.    Used to make bile salts (digestion), hormones (testosterone and estrogen), and vitamin D

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proteins structure

Always: C, H, O, N

Sometimes: S and P

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monomer of amino acids

Amino acids

Joined by peptide bonds

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functions of proteins

Cell structure

Enzymes

Transport

Movement

Communication

Defense

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function of structural support proteins

Proteins provide support and structure to cells and tissues.


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function of enzymes/catalysts (proteins)

Proteins speed up chemical reactions in the body.


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function of transportation proteins

Proteins transport substances throughout the body or across cell membranes.


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function of movement proteins

Proteins allow cells and body parts to move.


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function of communication proteins

Proteins help cells communicate with each other, often by acting as receptors or signaling molecules.


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function of defense proteins

Proteins help protect the body from harmful substances/pathogens, such as antibodies.


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monomer of proteins & how are they connected?

amino acid joined by peptide bonds via dehydration synthesis rxns


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amino acid structure

Amine group (-NH2)

Acid group (-COOH)

H+

R group

Variable


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enzymes lower ?

activation energy


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primary protein structure

Continuous strand of amino acid bound together by peptide bonds.

ii.     Linear

iii.   Proteins do not exist as linear chains of amino acids > no function


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Secondary structure of proteins


Patterns of hydrogen bonds that give either a twisty shape or a sheet shape.

1.     Twisty shape = alpha helix

2.     Sheet shape = beta-pleated sheet


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protein tertiary structure

3D shape formed by two secondary structures

  • fibrous

  • globular


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Fibrous Proteins

Strand-like

Hydrophobic

Stable

α-helices or β-sheets

Examples: Keratin, Elastin, Collagen

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Globular Proteins

Spherical

Hydrophilic

Sensitive to environmental changes

both α-helices and β-sheets

Ex: Antibodies, Hormones, Enzymes

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Proteins Quaternary Structure

  • How more than one polypeptide chain fits together to form a functional protein.

  • Not all proteins exhibit a quaternary structure only proteins made up of more than one polypeptide chain have quaternary structure.


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protein denaturation

  • Loss of their 3D shape > & function

  • Caused by ↑ temperatures, ↓ pH (acidity), Chemicals

  • Reversible if normal conditions are restored

  • more common


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Which type of protein (globular or fibrous) is more easily denatured?

Globular proteins because they fold into complex, compact shapes held together by weak, delicate bonds, shifts in temperature or pH easily disrupt their structure.

In contrast, fibrous proteins are highly resistant to denaturation because they form tough, tightly packed, rope-like structures stabilized by strong covalent cross-links.

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structure of nucleic acid

C, H, O, N and P

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monomer of nucleic acids

nucleotide

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structure of nucleotide

Nitrogenous base

Phosphate group

Sugar (monosaccharide)

>Ribose or Deoxyribose


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functions of nucleic acids

Store and transfer genetic information (DNA and RNA)

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ATP

1.     The main high energy compound in our bodies (though there are others).

2.     Structure

a.     Ribose

b.     Adenine

c.     3 phosphate groups

  • the bonds between the phosphate groups store tons of energy. When those bonds are broken via hydrolysis reactions, the energy that is released can be used to do cellular functions

1.     ATP is at the center of metabolism. It is the energy for our cells to carry out its functions


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The ? of glucose via glycolysis (a type of hydrolysis reaction) is used to make ATP.

catabolism