BIO 50 LEC - INORGANIC AND ORGANIC COMPOUNDS

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70 Terms

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Atom

smallest unit of an element

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Proton - + charged

Neutron - - no charge

Electron - — charged

Sub-atomic particles of an atom

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Elements

Fundamental units of matter

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matter

anything that occupies space and has mass (weight)

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  • Carbon

  • Oxygen

  • Hydrogen

  • Nitrogen

96% of the body is made from 4 elements

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Electron Configuration

- chemical behavior of an atom is determined by its electron configuration

– distribution of electrons in the atom’s electron shell

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Covalent bond

Sharing of valence electrons

<p>Sharing of valence electrons</p>
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Ionic bond

• Unequal sharing of electrons

• Salts

<p>• Unequal sharing of electrons</p><p> • Salts</p>
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Hydrogen bond

• Weak chemical bonds

• Hydrogen is attracted to negative portion of polar molecules

<p>• Weak chemical bonds</p><p> • Hydrogen is attracted to negative portion of polar molecules</p>
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Organic Compounds

• Contain carbon

• Most are covalently bond

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Inorganic Compounds

• Lack carbon

• Tend to be simpler compounds

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Intracellular

fluid located within cells

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Extracellular

fluid outside body cells

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High specific heat

amount of heat that must be lost for 1g of that substance to change its temperature by 1ºC

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High surface tension

how difficult it is to stretch or break the surface of a liquid

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High heat of vaporization

  • quantity of heat a liquid must absorb for 1g of it to be converted from liquid to the gaseous state

  • 100ºC

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Expansion upon freezing

  • achieves maximum density at 4ºC

  • at 0ºC, water becomes locked into a crystallline lattice

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Versatile solvent

  • allows aqueous solutions of life

  • contains a diversity of dissolved substances

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Dehydration

It removes a water molecule, forming a new bond.

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Hydrolysis

adds a water molecule, breaking a bond

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SALTS (Ions)

  • charged particles; electrolytes

  • important for nerve impulse conduction; muscle contraction

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Acids

a substance that increases the hydrogen ion concentration of a solution

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Bases

a substance that reduces the hydrogen ion concentration of a solution

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pH

measures the relative concentration of hydrogen ions

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neutral

pH 7

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acidic

pH below 7

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basic

pH above 7

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Buffers

substances that minimize changes in the concentration of H+ and OH – in a solution

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• carbohydrates

• lipids/ fats

• proteins

• Nucleotides and nucleic acids

Organic compounds

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Polymers

large molecules consisting of many identical or similar subunits strung together

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Carbohydrates

  • composed of C : H : O in a 1 : 2 : 1 ratio

  • Importance:

    - energy source

    - transportable forms of energy

    - structural material

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• Monosaccharides

• Disaccharides

• Polysaccharides

Carbohydrates are classified according to size. Classification:

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monosaccharide

simple sugar

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disaccharide

double sugar

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polysaccharide

starch

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  • triglycerides (neutral fats)

  • steroids

Common lipids in the human body

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Neutral fats (triglycerides)

• Found in fat deposits

• Source of stored energy

• Composed of three fatty acids and one glycerol molecule

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Saturated fatty acids

fatty acids that contain only single covalent bonds

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Unsaturated fatty acids

fatty acids that contain one or more double covalent bonds

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Steroids

• Include cholesterol, bile salts, vitamin D, and some hormones

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Cholesterol

the basis for all steroids made in the body

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Proteins

-50% dry weight of cell

- polymers of amino acid

- peptide bond

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Amino Acid

- possess both carboxyl and amino groups

- R-side chain

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  • phenylalanine

  • leucine

  • isoleucine

  • methionine

  • tryptophan

  • proline

  • threonine

  • alanine

  • cysteine

  • glycine

  • valine

  • serine

  • arginine

20 Amino Acids

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glycine

simplest amino acid

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aspartic acid

an acidic amino acid

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lysine

basic amino acid

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cysteine

sulfur-containing amino acid

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hydrophilic head, hydrophobic tail

phospholipid has ____ head and ______ tail

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structural proteins

  • the function of this type of protein is support

  • example: insects and spiders use silk fibers to make their cocoons and webs, respectively. Collagen and elastin provide a fibrous framework in animal connective tissues. Keratin is the portion of hair, horns, feathers, and other skin appendages.

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storage proteins

  • the function of this type of protein is to store amino acids

  • Example: Ovalbumin is the protein of egg white, used as an amino acid source for the developing embryo. Casein, the protein of milk, is the major source of amino acids for baby mammals. Plant have storage proteins in their seeds.

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transport proteins

  • the function of this type of protein is transport other substances

  • Example: Hemoglobin, the iron-containing protein of vertebrate blood, transports oxygen from the lung to other parts of the body. Other proteins transport molecules aross cell membranes.

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hormonal proteins

  • the function of this type of protein: coordination of an organism’s activities

  • Example: Insulin, a hormone secreted by the pancreas, help regulate the concentration of sugar in the blood of vertebrates.

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Receptor Proteins

  • the function of this type of protein: response of cll to chemical stimuli

  • Example: Receptor built into the membrane of a nerve cll detect chemical signals rlased by other nerve cells.

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Contractile Proteins

  • the function of this type of protein: movement

  • Example: Actin and myosin are responsible for the movement of muscles. Other proteins are responsible for the undulations of the organelles called cilia and flagella.

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defensive proteins

  • the function of this type of protein: protection against disease

  • Example: Antibodies combat bacteria and viruses.

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Enzymatic proteins

  • the function of this type of protein: selective acceleration of chemical reactions

  • Example: digestive enzymes catalyze the hydrolysis of the polymers in food

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  • Primary Structure (1º)

  • Secondary Structure (2º)

  • Tertiary Structure (3º)

  • Quarternary Structure (4º

Levels of Protein Structure

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Primary Structure (1º)

unique sequence of amino acids

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Secondary Structure (2º)

repeated coiling or folding of the primary structure

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Tertiary Structure (3º)

irregular contortions of the 2º formed by the bonds of the side chains (R groups) of the amino acid

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Quarternary Structure (4º)

overall protein structure that results from the aggregation of several polypeptide subunits.

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Globular Proteins

  • Also known as functional proteins

  • Function as antibodies or enzymes

  • Can be denatured

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Enzymes

  • Acts as biological catalysts

  • Increase the rate of chemical reactions

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nitrogenous base; 5-C sugar; phosphate group

Nucleotides

(basic structure)

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Adenosine Triphosphate (ATP)

  • Chemical energy used by all cells

  • Replenished by oxidation of food fuels

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DNA and RNA

storage, transmission of genetic information

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purines (e.g. adenine and guanine)

this has double rings made of carbon and nitrogen

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pyrimidines (e.g. cytosine, thymine, uracil)

only has one ring made up of (4) carbons and (2) nitrogen atoms

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phosphate, sugar, adenine

adenine nucleotide structure