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ESSENTIAL KNOWLEDGE 4.A.1: The subcomponents of biological molecules and their sequence determine the properties of that molecule.

Essential knowledge 4.A.1:

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Essential knowledge 4.A.1:. The subcomponents of biological molecules and their sequence determine the properties of that molecule. Macromolecules. Bozeman Biology: https://www.youtube.com/watch?v=PYH63o10iTE&list=PL8GOEDwLwlIOiSrWJuCzUxJ_zMemyYDDZ&index=5 - PowerPoint PPT Presentation

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Page 1: Essential knowledge 4.A.1:

ESSENTIAL KNOWLEDGE 4.A.1:

The subcomponents of biological molecules and their

sequence determine the properties of that molecule.

Page 3: Essential knowledge 4.A.1:

Structure and function of polymers are derived from the way their monomers are assembled.

Page 4: Essential knowledge 4.A.1:

Polymers Covalent monomers Condensation

reaction (dehydration reaction): One monomer provides a hydroxyl group while the other provides a hydrogen to form a water molecule

Hydrolysis:bonds

between monomers are broken by adding water (digestion)

Page 5: Essential knowledge 4.A.1:

Carbohydrates Monosaccharides

CH2O formula; √ multiple hydroxyl (-OH) groups and 1 carbonyl (C=O) group:

aldehyde (aldoses) sugar ketone sugar √ cellular respiration;

√ raw material for amino acids and fatty acids

Page 6: Essential knowledge 4.A.1:

Carbohydrates Disaccharides

glycosidic linkage (covalent

bond) between 2

monosaccharides;

covalent bond by dehydration reaction

Sucrose (table sugar) most common disaccharide

Page 7: Essential knowledge 4.A.1:

Carbohydrates Polysaccharides Energy Storage: Plants: starch (glucose

monomers) Animals: glycogen

Polysaccharides Structural in function:

Plants: Cellulose Animals:Chitin (found

in the exoskeleton of arthropods; also in the cell walls of fungi;

Page 8: Essential knowledge 4.A.1:

Carbohydrates Summary: Carbohydrates are

composed of sugar monomers whose structures and bonding with each other by dehydration synthesis determine the properties and functions of the molecules.

Illustrative examples include: cellulose versus starch.

Page 9: Essential knowledge 4.A.1:

Lipids No polymers; glycerol and fatty acid Fats, phospholipids, steroids Hydrophobic; H bonds in water

exclude fats Carboxyl group = fatty acid Non-polar C-H bonds in fatty acid

‘tails’ Ester linkage: 3 fatty acids to 1

glycerol (dehydration formation) Triacyglycerol (triglyceride) Saturated vs. unsaturated fats;

single vs. double bonds

Page 10: Essential knowledge 4.A.1:

Phospholipids 2 fatty acids instead

of 3 (phosphate group)

‘Tails’ hydrophobic; ‘heads’ hydrophilic

Micelle (phospholipid droplet in water)

Bilayer (double layer); cell membranes

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Steroids Lipids with 4 fused

carbon rings Ex: cholesterol:

cell membranes;precursor for other

steroids (sex hormones); atherosclerosis

Page 12: Essential knowledge 4.A.1:

Lipids Summary In general, lipids are

nonpolar; however, phospholipids exhibit structural properties, with polar regions that interact with other polar molecules such as water, and with nonpolar regions where differences in saturation determine the structure and function of lipids.

Page 13: Essential knowledge 4.A.1:

Proteins Importance: instrumental in nearly everything organisms

do; 50% dry weight of cells; most structurally sophisticated molecules known

Monomer: amino acids (there are 20) ~ carboxyl (-COOH) group, amino group (NH2), H atom, variable group (R)….

Variable group characteristics: polar (hydrophilic), nonpolar (hydrophobic), acid or base

Three-dimensional shape (conformation) Polypeptides (dehydration reaction): peptide

bonds~ covalent bond; carboxyl group to amino group (polar)

Page 14: Essential knowledge 4.A.1:

Protein Structure

•Primary•Secondary•Tertiary•Quaternary

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Primary Structure Conformation:

Linear structure Molecular Biology:

each type of protein has a unique primary structure of amino acids

Ex: lysozyme Amino acid

substitution:hemoglobin; sickle-cell anemia

Page 16: Essential knowledge 4.A.1:

Secondary Structure

Conformation: coils & folds

(hydrogen bonds) Alpha Helix:

coiling; keratin Pleated Sheet:

parallel; silk

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Tertiary Structure

Conformation: irregular contortions from R group bonding√hydrophobic√disulfide bridges√hydrogen bonds √ionic bonds

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Quaternary Structure

Conformation: 2 or more polypeptide chains aggregated into 1 macromolecule

Ex: collagen (connective tissue)

hemoglobin

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Types of Proteins Structural Protein Storage Proteins Transport Proteins Receptor Proteins Contractile Defensive Enzymes Signal Sensory Gene Regulator

Page 20: Essential knowledge 4.A.1:

Protein Summary In proteins, the specific order of amino acids in

a polypeptide (primary structure) interacts with the environment to determine the overall shape of the protein, which also involves secondary tertiary and quaternary structure and, thus, its function.

The R group of an amino acid can be categorized by chemical properties (hydrophobic, hydrophilic and ionic), and the interactions of these R groups determine structure and function of that region of the protein.

Page 21: Essential knowledge 4.A.1:

Nucleic Acids, I Deoxyribonucleic acid (DNA) Ribonucleic acid (RNA) DNA->RNA->protein Polymers of nucleotides

(polynucleotide):nitrogenous base

pentose sugarphosphate group

Nitrogenous bases:pyrimidines~cytosine,

thymine, uracil purines~adenine, guanine

Page 22: Essential knowledge 4.A.1:

Nucleic Acids

Pentoses:√ribose (RNA)√deoxyribose (DNA)√nucleoside (base + sugar)

Polynucleotide:√phosphodiester linkages (covalent); phosphate + sugar

Page 23: Essential knowledge 4.A.1:

Nucleic Acids

Inheritance based on DNA replication

Double helix (Watson & Crick - 1953)

H bonds~ between paired bases

van der Waals~ between stacked bases

A to T; C to G pairing Complementary

Page 24: Essential knowledge 4.A.1:

Nucleic Acids Summary In nucleic acids, biological information is

encoded in sequences of nucleotide monomers. Each nucleotide has structural components:

a five-carbon sugar (deoxyribose or ribose), a phosphate and a nitrogen base (adenine, thymine, guanine, cytosine or uracil).

DNA and RNA differ in function and differ slightly in structure, and these structural differences account for the differing functions.

Page 25: Essential knowledge 4.A.1:

Directionality influences structure and function of the polymer.

Examples are found in DNA, Proteins and Carbohydrates on the following slides.

Page 27: Essential knowledge 4.A.1:

Proteins 2. Proteins have an amino (NH2) end and a

carboxyl (COOH) end, and consist of a linear sequence of amino acids connected by the formation of peptide bonds by dehydration synthesis between the amino and carboxyl groups of adjacent monomers.

Page 28: Essential knowledge 4.A.1:

Carbohydrates 3. The nature of the bonding between

carbohydrate subunits determines their relative orientation in the carbohydrate, which then determines the secondary structure of the carbohydrate.