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doodlebob

D. Compounds

  • Compound occurs as result of 2 or more individual elements combining in a fixed ratio 

    • Different properties of individual elements

    • Formed by chemical reaction

  • Bonds that hold compounds together

    • Ionic bonds TRANSFERRED

      • nonmetal+metal

      • One or more electrons is transferred from one atom to another

      • One atom loses electrons (becomes positively charged) while the other gains electrons (becomes negatively charged)

      • Results from attraction of two oppositely charged ions

      • Cation has a positive charge

      • Anion has a negative charge

      • Cation and anion form to create ionic bond

    • Covalent bonds SHARED

      • nonmetal+nonmetal

      • Molecule consists of 2 or more atoms held together by covalent bonds

      • Formed when electrons are shared between atoms

      • In nonpolar covalent bond, electrons are shared equally

      • In polar covalent bond, electrons are shared unequally

      • In a single covalent bond, one pair of electrons is shared

        • Double covalent when 2 pairs are shared, etc. 

      • Structural formula used to represent atoms and bonding

        • Ex. H-H

      • Molecular formula abbreviates structural formula

        • Ex. H2

        • Electronegativity is an atom’s attraction for the atoms in a covalent bond

          • The more electronegative an atom, the more strongly it pulls shared electrons toward itself

    • Hydrogen bonds 

      • Hydrogen atom covalently bonds to one electronegative ato is also attracted to another electronegative atom

      • In living cells, hydrogen bonds are usually oxygen or other nitrogen atoms

    • Van der Waals Interactions

      • Weakest

      • If electrons are distributed asymmetrically in molecules or atoms, they can result in “hot spots” of positive or negative charge

      • Attractions between molecules that are close together as a result of these charges

        • How geckos climb

E. Water: The Versatile Molecule

  • In water, electrons are not shared equally in the bonds between hydrogen and oxygen

    • Hydrogen atoms have a partial positive charge while oxygen atoms has a partial negative charge

      • Water is polar

  • Hydrogen bonds

    • Weak attractions that result of water’s polarity

      • Positive end of another polar molecule attracted to oxygen negative charge, and vice versa with the hydrogen end

      • Hydrogen atom covalently bonded to one electronegative atom is also attracted to another electronegative atom

      • Weak Individually, but strong on a larger scale

hydrogen bond= water + water

  • Lends watermany special properties

    • Cohesion

      • Tendency for water to stick to water

      • Important during transpiration

        • Water evaporates, pulls other water molecules with it, pulling all the way down from leaves to roots

    • Adhesion

      • Tendency of water to stick to other substances

      • Cohesion + Adhesion = capillary action

        • Allows water to flow up roots/trunks/branches of trees in thin vessels

    • Surface tension

      • Results from cohesion of water molecules

      • Ex. water striders can sit on top of water without sinking

    • High heat capacity

      • Heat CApacity=ability of a substance to resist temperature changes

      • Keeps ocean temperatures stable

      • Allows organisms to keep constant body temperature, since most life forms are mostly made up of water

      • Heat is absorbed  when hydrogen bonds break, released when hydrogen bonds form

    • High heat of vaporization

      • Heat a liquid must absorb for 1g to be converted to gas

      • Evaporative cooling

        • As a liquid evaporates, its remaining surface cools

          • How sweat works to cool body down

    • Expansion on freezing

      • Lattice structure of ice causes water to expand on freezing

      • Allows ice to float on top of lakes in winter

        • Animal life can live beneath ice

    • Versatility as a solvent

      • Solution is a liquid that is a homogenous mix of substances

      • Solvent is the dissolving agent of a solution

      • Solute is the substance that is dissolved

      • Aqueous solution is one where water is the solvent

      • Polarity of water allows it to be a versatile solvent

        • Can form hydrogen bonds easily

        Hydrophobic substances do not dissolve in water, but hydrophilic ones will

  • Carbohydrates

    • Contain carbon,  hydrogen, and oxygen in a 1:2:1 ratio

    • Monosaccharides

      • Most common are glucose and fructose

        • Glucose

          • Most abundant

          • Part of food humans eat

          • Made by plants during photosynthesis

            • Broken down to release energy

        • Fructose

          • Common sugar in fruits

        • Can be depicted as either straight or rings

  • 6 carbon-sugars

    • Formula: C6H12O6

  • Disaccharides

    • 1 monosaccharide+1 monosaccharide=1 Disaccharide

    • Formed by dehydration synthesis

      • Aka condensation

      • Hydrogen (-H) from one sugar combines with hydroxyl group (-OH) of another sugar molecule to create water as byproduct

  • Bond is called glycosidic linkage

  • Broken apart by hydrolysis

    • Reverse of dehydration

    • Water is used to break apart glycosidic linkage

  • Polysaccharides

    • Repeated units of monosaccharides

    • Most common

      • Starch

        • Stores sugar in plants

        • Made up of alpha-glucose molecules

      • Cellulose

        • Made up of ß-glucose molecules

        • Chitin

          • Structural molecule in walls of fungi/arthropod exoskeletons

          • Used as surgical thread since it breaks down in body

      • Glycogen

        • Stores sugar in animals

  • Proteins

    • Amino acids=monomer of proteins

      • 20 kinds of naturally occurring amino acids

    • Contain:

      • Carbon

      • Hydrogen

      • Oxygen

      • Nitrogen

    • 4 parts of an amino acid centered around a central carbon

      • Amino group (-NH2)

      • Carboxyl group (-COOH)

      • Hydrogen

      • R group

        • Aka side chain

        • Interchangeable

        • Vary in composition, polarity, charge, shape depending on specific side chain

        • Polar R groups point outward, hydrophobic R groups point inward

    • Polypeptides

      • Amino acid + amino acid= dipeptide

        • Formed by dehydration synthesis

        • Bond is called a peptide bond

        • Multiple amino acids= polypeptide

          • Once a polypeptide chain twists and folds on itself, it forms a 3D structure called a protein

  • Higher protein structure (4 levels total)

    • Primary structure

      • Linear sequence of amino acids

      • Covalent (peptide) bonds

    • Secondary structure

      • Protein beings to twist--2 options

        • Forms a coil (alpha-helix)

        • Zigzagging pattern (known as beta-pleated sheets)

      • Shape depends on R-group

      • Formed by amino acids that interact with other amino acids closeby in the primary structure

      • Hydrogen bonds between carbonyl and amino group

      • Interactions between amino and carboxyl groups of protein backbone

      • After secondary structure forms, formerly distant amino acids are now closeby--tertiary structure can form

    • Tertiary structure

      • Can be both alpha and beta helix/sheets within structure

      • Covalent disulfide bridge often stabilizes structure

      • Bonds between R groups

        • Hydrogen bonds

        • Ionic bonds

        • Disulfide bridges

        • Hydrophobic interactions

    • Quaternary structure

      • Several different polypeptide chains sometimes interact with each other

      • Same bonds as above, but between peptide chains rather than between R groups

    • Mistakes in structure can denature a protein

      • Change of shape=change of function

        • Ex. pH or heat can denature protein

    • Protein folding can involve chaperone proteins (chaperonins)

      • Help protein fold properly

      • Make process more efficient







8 kinds of Proteins

Name

Function

Enzymatic

Selective acceleration of chemical reactions

Defensive

Protection against disease

storage

Storage of amino acids

transport

Transport of substances

hormonal

Coordination of organism’s biological activities

receptor

Response of cell to chemical stimuli

contractile/motor

movement

Structural

support


  • Lipids

    • Like carbs, consist of carbon, hydrogen and oxygen, but not in a fixed ratio

    • Do not form polymers

    • Little-no affinity for water

      • Hydrophobic due to nonpolar covalent bonds of hydrocarbon

    • Common examples:

      • Triglycerides

        • Glycerol molecule+3 fatty acid chains attached

          • Fatty acid chain is mostly a long chain of carbons where each carbon is covered in hydrogen; One end of the chain has a carboxyl group (-COOH)

            • Vary in length and #/location(s) of double bonds

          • Glycerol is a 3-carbon alcohol with a hydroxyl group attached to each carbon 

        • Fats separate from water because water forms hydrogen bonds with itself while excluding the fats

        • In order to be made, each of the carboxyl groups of the 3 fatty acids must react with one of the 3 hydroxyl groups of the glycerol molecule via dehydration synthesis

          • bond=ester linkage

        • Saturated fatty acid

          • No double bond

          • Carbon chain completely filled (“saturated”) with hydrogen

          • Usually solid at room temp.

        • Unsaturated fatty acid

          • Double bond along carbon chain, causing a bend

            • Bend allows triglyceride to become LESS dense, making it liquid at room temperature

          • Polyunsaturated fatty acid has multiple double bonds within the fatty acid, causing many bends

  • Phospholipids

  • 2 fatty acid “tails” + 1 negatively charged phosphate “head”


  • Tails are hydrophobic, while head is hydrophilic (negative charge on head attracts polar water)

    • Amphipathic molecule (molecule that is both polar and nonpolar)

  • In water, phospholipids self-assemble into a “bilayer arrangement” 

    • Hydrophobic tails face towards interior

    • Found in cell membranes

  • Steroids

    • Cholesterol

      • 4-ringed molecule dispersed throughout membrane

        • Maintains membrane stability

          • Increases membrane fluidity at lower temperatures by disrupting close packing

          • Decreases fluidity at high temperatures through its constant movement

  • Nucleic Acids

    • Contain carbon, hydrogen, oxygen, nitrogen, and phosphorous

    • Structure

      • Nitrogenous base

      • Pentose sugar

      • Phosphate group

      • Portion of nucleotide w/o phosphate group is called nucleoside

    • Store, transmit, and help expres hereditary information

    • monomer=nucleotides

    • Amino acid sequence of a polypeptide is programmed by a unit of inheritance called a gene

      • Made up of DNA

    • Deoxyribonucleic acid (DNA)

      • sugar=deoxyribose

      • Contains genetic/hereditary information

      • Provides directions for its own replication

      • Directs synthesis of messenger RNA (mRNA), and through mRNA, controls protein synthesis

        • Occurs on ribosomes

    • Ribonucleic acid (RNA)

      • sugar=ribose

      • Essential for protein synthesis

    • 2 families of nitrogenous bases

      • Pyrimidines

        • Single 6-membered ring

        • Ex.

          • Cytosine

          • Thymine (only DNA

          • Uracil (only RNA)

      • Purines

        • 6-membered ring fused to a 5-membered ring

        • Ex.

          • Adenine

          • Guanine

    • Nucleotide Polymers

      • Nucleotide polymers linked together to build a polynucleotide

      • Adjacent nucleotides are joined by covalent bonds that form between the -OH group on the 3’ carbon of one nucleotide and the phosphate on the 5’ carbon on the next

        • Links create a backbone of sugar-phosphate units with nitrogenous bases as appendages

      • RNA molecules usually exist as single polypeptide chains

      • DNA molecules have 2 polynucleotides spiraling around an imaginary axis, forming a double helix

        • Two backbones run in opposite 5’→3’ directions from each other (antiparallel)

        • One DNA molecule contains many genes

        • Nitrogenous bases pair up and form hydrogen bonds

          • Adenine-Thymine

          • Guanine-Cytosine

          • Complementary base pairing

          • In RNA, thymine is replaced by uracil, so A and U pair








Macromolecule

Monomer

Polymer

Linkage Bond

Carbohydrates

Monosaccharide (ex. Glucose)

Polysaccharide (ex. Starch, glycogen, cellulose)

Glycosidic linkage

Proteins

Amino Acid (Ex. Glycine)

Polypeptide (ex. actin)

Peptide bond

Nucleic Acids

Nucleotides (ex. Adenine, thymine, guanine, cytosine)

DNA or RNA

Sugar-phosphate phosphodiester bonds

Lipids

Not a true polymer, but often contains chains of carbons with hydrogens

Triglycerides, Phospholipids, cholesterol

Ester bonds

F. Origins of the Earth

  • Alexander Oparin and J. B. S. Haldane proposed that the primitive atmosphere contained the following gases:

    • Methane (CH4)

    • Ammonia (NH3)

    • Hydrogen (H2)

    • Water (H2O)

    • No free oxygen (O2)

      • No oxidation/reduction

      • Rocks do not release oxygen through weathering

    • Gases collided, producing chemical reactions that eventually led to the organic molecules we know today

    • Substantial support until 1953

  • 1953, Stanley Miller and Harold Urey simulated the conditions of primitive Earth in a lab,

    • Put theoried gases into flask, struck them with electrical charges to simulate lightning, and organic compounds similar to amino acids appeared

  • Current theory of the origin of life suggests 4 main stages

    • 1. Formation of amino acids

    • 2. Monomers form polymers

    • 3. Enclosure of small organic molecules into larger ones

    • 4. Self-replicating molecules that can direct synthesis of other organic substances

      • Energy sources for early organic synthesis

        • Lightning 

        • Volcanic eruptions

  • RNA world hypothesis

    • Original life-forms were simple molecules of RNA

      • RNA not restricted to double helix

      • RNA capable of replicating and passing genes

    • Complex organic compounds must have formed via dehydration synthesis

      • Organic compounds then used as food by cells

        • Simple cells evolved into complex cells

doodlebob

D. Compounds

  • Compound occurs as result of 2 or more individual elements combining in a fixed ratio 

    • Different properties of individual elements

    • Formed by chemical reaction

  • Bonds that hold compounds together

    • Ionic bonds TRANSFERRED

      • nonmetal+metal

      • One or more electrons is transferred from one atom to another

      • One atom loses electrons (becomes positively charged) while the other gains electrons (becomes negatively charged)

      • Results from attraction of two oppositely charged ions

      • Cation has a positive charge

      • Anion has a negative charge

      • Cation and anion form to create ionic bond

    • Covalent bonds SHARED

      • nonmetal+nonmetal

      • Molecule consists of 2 or more atoms held together by covalent bonds

      • Formed when electrons are shared between atoms

      • In nonpolar covalent bond, electrons are shared equally

      • In polar covalent bond, electrons are shared unequally

      • In a single covalent bond, one pair of electrons is shared

        • Double covalent when 2 pairs are shared, etc. 

      • Structural formula used to represent atoms and bonding

        • Ex. H-H

      • Molecular formula abbreviates structural formula

        • Ex. H2

        • Electronegativity is an atom’s attraction for the atoms in a covalent bond

          • The more electronegative an atom, the more strongly it pulls shared electrons toward itself

    • Hydrogen bonds 

      • Hydrogen atom covalently bonds to one electronegative ato is also attracted to another electronegative atom

      • In living cells, hydrogen bonds are usually oxygen or other nitrogen atoms

    • Van der Waals Interactions

      • Weakest

      • If electrons are distributed asymmetrically in molecules or atoms, they can result in “hot spots” of positive or negative charge

      • Attractions between molecules that are close together as a result of these charges

        • How geckos climb

E. Water: The Versatile Molecule

  • In water, electrons are not shared equally in the bonds between hydrogen and oxygen

    • Hydrogen atoms have a partial positive charge while oxygen atoms has a partial negative charge

      • Water is polar

  • Hydrogen bonds

    • Weak attractions that result of water’s polarity

      • Positive end of another polar molecule attracted to oxygen negative charge, and vice versa with the hydrogen end

      • Hydrogen atom covalently bonded to one electronegative atom is also attracted to another electronegative atom

      • Weak Individually, but strong on a larger scale

hydrogen bond= water + water

  • Lends watermany special properties

    • Cohesion

      • Tendency for water to stick to water

      • Important during transpiration

        • Water evaporates, pulls other water molecules with it, pulling all the way down from leaves to roots

    • Adhesion

      • Tendency of water to stick to other substances

      • Cohesion + Adhesion = capillary action

        • Allows water to flow up roots/trunks/branches of trees in thin vessels

    • Surface tension

      • Results from cohesion of water molecules

      • Ex. water striders can sit on top of water without sinking

    • High heat capacity

      • Heat CApacity=ability of a substance to resist temperature changes

      • Keeps ocean temperatures stable

      • Allows organisms to keep constant body temperature, since most life forms are mostly made up of water

      • Heat is absorbed  when hydrogen bonds break, released when hydrogen bonds form

    • High heat of vaporization

      • Heat a liquid must absorb for 1g to be converted to gas

      • Evaporative cooling

        • As a liquid evaporates, its remaining surface cools

          • How sweat works to cool body down

    • Expansion on freezing

      • Lattice structure of ice causes water to expand on freezing

      • Allows ice to float on top of lakes in winter

        • Animal life can live beneath ice

    • Versatility as a solvent

      • Solution is a liquid that is a homogenous mix of substances

      • Solvent is the dissolving agent of a solution

      • Solute is the substance that is dissolved

      • Aqueous solution is one where water is the solvent

      • Polarity of water allows it to be a versatile solvent

        • Can form hydrogen bonds easily

        Hydrophobic substances do not dissolve in water, but hydrophilic ones will

  • Carbohydrates

    • Contain carbon,  hydrogen, and oxygen in a 1:2:1 ratio

    • Monosaccharides

      • Most common are glucose and fructose

        • Glucose

          • Most abundant

          • Part of food humans eat

          • Made by plants during photosynthesis

            • Broken down to release energy

        • Fructose

          • Common sugar in fruits

        • Can be depicted as either straight or rings

  • 6 carbon-sugars

    • Formula: C6H12O6

  • Disaccharides

    • 1 monosaccharide+1 monosaccharide=1 Disaccharide

    • Formed by dehydration synthesis

      • Aka condensation

      • Hydrogen (-H) from one sugar combines with hydroxyl group (-OH) of another sugar molecule to create water as byproduct

  • Bond is called glycosidic linkage

  • Broken apart by hydrolysis

    • Reverse of dehydration

    • Water is used to break apart glycosidic linkage

  • Polysaccharides

    • Repeated units of monosaccharides

    • Most common

      • Starch

        • Stores sugar in plants

        • Made up of alpha-glucose molecules

      • Cellulose

        • Made up of ß-glucose molecules

        • Chitin

          • Structural molecule in walls of fungi/arthropod exoskeletons

          • Used as surgical thread since it breaks down in body

      • Glycogen

        • Stores sugar in animals

  • Proteins

    • Amino acids=monomer of proteins

      • 20 kinds of naturally occurring amino acids

    • Contain:

      • Carbon

      • Hydrogen

      • Oxygen

      • Nitrogen

    • 4 parts of an amino acid centered around a central carbon

      • Amino group (-NH2)

      • Carboxyl group (-COOH)

      • Hydrogen

      • R group

        • Aka side chain

        • Interchangeable

        • Vary in composition, polarity, charge, shape depending on specific side chain

        • Polar R groups point outward, hydrophobic R groups point inward

    • Polypeptides

      • Amino acid + amino acid= dipeptide

        • Formed by dehydration synthesis

        • Bond is called a peptide bond

        • Multiple amino acids= polypeptide

          • Once a polypeptide chain twists and folds on itself, it forms a 3D structure called a protein

  • Higher protein structure (4 levels total)

    • Primary structure

      • Linear sequence of amino acids

      • Covalent (peptide) bonds

    • Secondary structure

      • Protein beings to twist--2 options

        • Forms a coil (alpha-helix)

        • Zigzagging pattern (known as beta-pleated sheets)

      • Shape depends on R-group

      • Formed by amino acids that interact with other amino acids closeby in the primary structure

      • Hydrogen bonds between carbonyl and amino group

      • Interactions between amino and carboxyl groups of protein backbone

      • After secondary structure forms, formerly distant amino acids are now closeby--tertiary structure can form

    • Tertiary structure

      • Can be both alpha and beta helix/sheets within structure

      • Covalent disulfide bridge often stabilizes structure

      • Bonds between R groups

        • Hydrogen bonds

        • Ionic bonds

        • Disulfide bridges

        • Hydrophobic interactions

    • Quaternary structure

      • Several different polypeptide chains sometimes interact with each other

      • Same bonds as above, but between peptide chains rather than between R groups

    • Mistakes in structure can denature a protein

      • Change of shape=change of function

        • Ex. pH or heat can denature protein

    • Protein folding can involve chaperone proteins (chaperonins)

      • Help protein fold properly

      • Make process more efficient







8 kinds of Proteins

Name

Function

Enzymatic

Selective acceleration of chemical reactions

Defensive

Protection against disease

storage

Storage of amino acids

transport

Transport of substances

hormonal

Coordination of organism’s biological activities

receptor

Response of cell to chemical stimuli

contractile/motor

movement

Structural

support


  • Lipids

    • Like carbs, consist of carbon, hydrogen and oxygen, but not in a fixed ratio

    • Do not form polymers

    • Little-no affinity for water

      • Hydrophobic due to nonpolar covalent bonds of hydrocarbon

    • Common examples:

      • Triglycerides

        • Glycerol molecule+3 fatty acid chains attached

          • Fatty acid chain is mostly a long chain of carbons where each carbon is covered in hydrogen; One end of the chain has a carboxyl group (-COOH)

            • Vary in length and #/location(s) of double bonds

          • Glycerol is a 3-carbon alcohol with a hydroxyl group attached to each carbon 

        • Fats separate from water because water forms hydrogen bonds with itself while excluding the fats

        • In order to be made, each of the carboxyl groups of the 3 fatty acids must react with one of the 3 hydroxyl groups of the glycerol molecule via dehydration synthesis

          • bond=ester linkage

        • Saturated fatty acid

          • No double bond

          • Carbon chain completely filled (“saturated”) with hydrogen

          • Usually solid at room temp.

        • Unsaturated fatty acid

          • Double bond along carbon chain, causing a bend

            • Bend allows triglyceride to become LESS dense, making it liquid at room temperature

          • Polyunsaturated fatty acid has multiple double bonds within the fatty acid, causing many bends

  • Phospholipids

  • 2 fatty acid “tails” + 1 negatively charged phosphate “head”


  • Tails are hydrophobic, while head is hydrophilic (negative charge on head attracts polar water)

    • Amphipathic molecule (molecule that is both polar and nonpolar)

  • In water, phospholipids self-assemble into a “bilayer arrangement” 

    • Hydrophobic tails face towards interior

    • Found in cell membranes

  • Steroids

    • Cholesterol

      • 4-ringed molecule dispersed throughout membrane

        • Maintains membrane stability

          • Increases membrane fluidity at lower temperatures by disrupting close packing

          • Decreases fluidity at high temperatures through its constant movement

  • Nucleic Acids

    • Contain carbon, hydrogen, oxygen, nitrogen, and phosphorous

    • Structure

      • Nitrogenous base

      • Pentose sugar

      • Phosphate group

      • Portion of nucleotide w/o phosphate group is called nucleoside

    • Store, transmit, and help expres hereditary information

    • monomer=nucleotides

    • Amino acid sequence of a polypeptide is programmed by a unit of inheritance called a gene

      • Made up of DNA

    • Deoxyribonucleic acid (DNA)

      • sugar=deoxyribose

      • Contains genetic/hereditary information

      • Provides directions for its own replication

      • Directs synthesis of messenger RNA (mRNA), and through mRNA, controls protein synthesis

        • Occurs on ribosomes

    • Ribonucleic acid (RNA)

      • sugar=ribose

      • Essential for protein synthesis

    • 2 families of nitrogenous bases

      • Pyrimidines

        • Single 6-membered ring

        • Ex.

          • Cytosine

          • Thymine (only DNA

          • Uracil (only RNA)

      • Purines

        • 6-membered ring fused to a 5-membered ring

        • Ex.

          • Adenine

          • Guanine

    • Nucleotide Polymers

      • Nucleotide polymers linked together to build a polynucleotide

      • Adjacent nucleotides are joined by covalent bonds that form between the -OH group on the 3’ carbon of one nucleotide and the phosphate on the 5’ carbon on the next

        • Links create a backbone of sugar-phosphate units with nitrogenous bases as appendages

      • RNA molecules usually exist as single polypeptide chains

      • DNA molecules have 2 polynucleotides spiraling around an imaginary axis, forming a double helix

        • Two backbones run in opposite 5’→3’ directions from each other (antiparallel)

        • One DNA molecule contains many genes

        • Nitrogenous bases pair up and form hydrogen bonds

          • Adenine-Thymine

          • Guanine-Cytosine

          • Complementary base pairing

          • In RNA, thymine is replaced by uracil, so A and U pair








Macromolecule

Monomer

Polymer

Linkage Bond

Carbohydrates

Monosaccharide (ex. Glucose)

Polysaccharide (ex. Starch, glycogen, cellulose)

Glycosidic linkage

Proteins

Amino Acid (Ex. Glycine)

Polypeptide (ex. actin)

Peptide bond

Nucleic Acids

Nucleotides (ex. Adenine, thymine, guanine, cytosine)

DNA or RNA

Sugar-phosphate phosphodiester bonds

Lipids

Not a true polymer, but often contains chains of carbons with hydrogens

Triglycerides, Phospholipids, cholesterol

Ester bonds

F. Origins of the Earth

  • Alexander Oparin and J. B. S. Haldane proposed that the primitive atmosphere contained the following gases:

    • Methane (CH4)

    • Ammonia (NH3)

    • Hydrogen (H2)

    • Water (H2O)

    • No free oxygen (O2)

      • No oxidation/reduction

      • Rocks do not release oxygen through weathering

    • Gases collided, producing chemical reactions that eventually led to the organic molecules we know today

    • Substantial support until 1953

  • 1953, Stanley Miller and Harold Urey simulated the conditions of primitive Earth in a lab,

    • Put theoried gases into flask, struck them with electrical charges to simulate lightning, and organic compounds similar to amino acids appeared

  • Current theory of the origin of life suggests 4 main stages

    • 1. Formation of amino acids

    • 2. Monomers form polymers

    • 3. Enclosure of small organic molecules into larger ones

    • 4. Self-replicating molecules that can direct synthesis of other organic substances

      • Energy sources for early organic synthesis

        • Lightning 

        • Volcanic eruptions

  • RNA world hypothesis

    • Original life-forms were simple molecules of RNA

      • RNA not restricted to double helix

      • RNA capable of replicating and passing genes

    • Complex organic compounds must have formed via dehydration synthesis

      • Organic compounds then used as food by cells

        • Simple cells evolved into complex cells

robot