AP Bio Chapter 5: The Structure and Function of Macromolecules

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Macromolecule

-Large Molecules composed of smaller molecules that are complex in their structure and function; most are polymers built from monomers

Four Classes of Life

- The class's organic molecules are polymers 1) Carbohydrates 2) Lipids 3) Proteins 4) Nucleic Acids

Polymer

Long molecules consisting of many similar building blocks called monomers

Specific Monomers

Make up each macromolecule; example- Amino Acids are monomers of proteins.

Synthesis of Polymers

Lose an H2O Molecule; expends energy to carry out reaction; need enzymes to speed reactions in cells; dehydration synthesis.

Dehydration Synthesis

How monomers form larger molecules by condensation reactions; monomers are linked by covalent bonds.

Water in dehydration synthesis

1 monomer provides -OH Hydroxyl Group and 1 monomer provides -H Hydrogen

Breakdown of Polymers

Hydrolysis can disassemble polymers; the reverse of dehydration synthesis; H2O is added

Example of the Breakdown of Polymers

Digestion: Food = polymers in the digestive track -> enzymes attack the polymers -> released monomers enter the bloodstream -> then enter into cells -> reassemble into new polymers that perform specific functions.

The arrangement of monomers into polymers

is the basis of each organisms uniqueness, even though organisms share the same limited number of monomer types

Cells

Made of 1000's of different macromolecules

Variations in Polymers

cause differences in organisms; 40-50 monomers can make a limitless number of polymers

Small set of monomers

can build an immense variety of polymers, for example proteins are made of 20 different amino acids in chains

Carbohydrates

serve as fuel and building material for cells; includes sugars and their polymers (starch, glucose, etc.)

Monosaccharides

simples of sugars, can be used for fuel, can be converted into other organic molecules, can be combined into polymers; generally have molecular formulas that are multiples of CH2O

most common monosaccharide and an Aldose

Glucose

structural trademarks of a sugar

Aldose and Ketose are types of sugars dependent on the location of the carbonyl group, C=O

size of carbon skeleton in monosaccharides

3 to 7

Dissaccharides

consist of two monosaccharides joined by a glycosidic linkage

glycosidic linkage

covalent bond formed between two monosaccharides by a dehydration reaction

Maltose

Example of disaccharides; Glucose + Glucose

Sucrose

Most prevalent sugar "Table Sugar"; Glucose + Fructose

Polysaccharides

polymers of sugars with 100s and 1000s of monomers; some serve as storage material and other building materials to protect cells and organisms

Starch

storage polysaccharides of plants and a polymer consisting entirely of glucose monomers; stored energy that can be removed later by hydrolysis. Ex. potatoes, grains, corn

Forms of Starch

Amylose: simplest form - linear/unbranched
Amylopectin: complex form - branched

Plastid

cellular structures that contain granules of starch for plants

Glycogen: storage Polysaccharide

A polymer of glucose that is the major storage form of glucose in animals; has many branches and is stored mainly in the liver and muscles cells; usually depleted within 24 hours unless replenished by food.

Cellulose: Structural Polysaccharide

a polymer of glucose; major component of cell walls; produced by the 100s and billions of tons annually by plants; most common compound on earth

Difference between starch and cellulose

starch: glucose monomers are in alpha configuration -OH group below #1 Carbon
cellulose: glucose monomers are in beta configuration -OH group above #1 Carbon
Glycosidic Linkages: starch-helical; cellulose straight

Structure of Cellulose

molecules are straight and -OH groups form hydrogen bonds with other -OH groups.

Microfibrils

paralllel cellulose molecules held by hydrogen bonds; they are cable like structures and strong building units.

Human Digestion of Cellulose

humans cannot digest it, but it rubs against the wall of our digestive tracts and causes us to produce mucus to pass food through out systems.

Cows and termites

have microbes(enzymes) in their first stomach that allows them to digest cellulose; termites have microbes in its gut allowing it to digest cellulose.

Chitin: structural polysaccharide

used by arthropods to build an exoskeleton; purely, its leathery, but becomes hardened when encrusted with calcium carbonate, CaCO3 ,a salt; cell wall of fungi

Chitin and Cellulose

glucose monomer of chitin has nitrogen-containing appendage.

Lipids

diverse group of hydrophobic molecules, one class of large biological molecules that doesn't consist of polymers b/c mostly hydrocarbons

Fats

large molecules assembled by small molecules by dehydration reactions; constructed from 2 types of smaller molecules: glycerol and fatty acids.

Fatty Acids

long carbon skeleton, usually 16 or 18 carbon atoms in length; at one end is a carboxyl group

Making a Fat: triacylglycerol/triglyceride

3 fatty acid molecules join to glycerol by an ester linkage

why fats are hydrophobic

non polar C-H bonds in hydrocarbon chains of fatter acids

Saturated Fatty Acids

have the maximum number of hydrogen atoms possible, no double bonds btwn carbon atoms in chain, saturated with hydrogen. Ex. animal fats = saturated = solid @ room temp.

Cardivascular disease

plaque build up in walls of blood vessels, allowing less and less blood to flow through and reduces resilience of the vessels.

unsaturated fatty acids

-have one or more double bonds due to the removal of hydrogen from the carbon skeleton
-removal of hydrogen causes a "kink" in its hydrocarbon chain wherever a cis double bond occurs.
-source from fish and plants

phospholipids

has only two fatty acids attached to glycerol and a phosphate group instead of a third fatty acid.

phospholipid structure

hydrocarbon tails and phosphate group head: hydrophilic head and hydrophobic tail.
form a bi-layer arrangement found in cell membranes where heads are on outside and tails are inside two layers of heads.

cell membrane

separates what goes into the cell from what goes out.

Steroids

lipids characterized by a carbon skeleton consisting of four fused rings

Cholesterol

steroid found in cell membranes and a precursor for other hormones and steroids to synthesize. high levels

high levels of cholesterol

BAD for your system; contributes to cardiovascular disease (atherosclerosis)

Proteins

many structure = wide range of functions;
do most of work in cells; 50% of dry mass of most cells

Protein Functions

Enzymatic, structural, storage, transport, hormonal, receptor, contractile and motor, defense

Enzymes

type of protein that acts as a catalyst, speeding up chemical reactions

polypeptides

polymers (chains) of amino acids; proteins consist of one or more polypeptides that foil and coil into specific shapes.

Amino Acids

organic molecules possessing both carboxyl group and amino groups

R Groups

variable group of an amino acid that differs with each amino acid

structure of Amino Acid

alpha carbon, assymetric carbon atom, at the center, and has four partners, amino group, carboxyl group, Hydrogen, and R group

Amino Acid Polymer

linked by peptide bonds; when 2 amino acids are side by side, the carboxyl group of one is adjacent to the amino group of another=an enzyme joins them in dehydration reaction

Peptide Bond

covalent bond resulting from the formation of an amino acid polymer

polypeptide

multitudes of peptide bond linkages

Fredrick Sanger

attended Cambridge University; determined the amino acid sequence of proteins needed on a cellular level while researching insulin

Protein Conformation and Function

proteins specific shape determines how it functions.

structure of protein

one or more polypeptides precisely twisted, folded, or coiled into a specific shape

Amino Acid Sequence

determines the 3D shape of the protein

Four Levels of Protein Structure

Primary, Secondary, Tertiary, and Quarternary

Primary Structure of Protein

the unique sequence of amino acids in a polymer.

Transthyretin

globular protein that transports vitamin A and thyroid hormones

Secondary Structure of Protein

the folding and coiling of the polypeptides into repeating configuration

alpha helix

a coil due to a hydrogen bond between every 4th amino acid

beta pleated sheet

polypeptide chains side by side connected by hydrogen bonds between backbones

core of globular proteins

alpha helix and beta pleated sheet

Tertiary structure

The overall three-dimensional 3D shape of a polypeptide resulting from interactions between the R Group/side chain and the amino acids

Hydrophobic Interaction

polypeptide folds into its functional shape, amino acids w/ hydrophobic side chains end up in clusters (core) of the protein.

H2Ophobic interaction and water molecules

h2o forms hydrogen bonds with each other and w/ hydrophilic parts of protein, in turn excluding nonpolar substances.

Quarternary Structure

The overall protein structure that results from the aggregation of two or more polypeptide subunits.

collagen

helical subunits intertwined in a triple helix makes it really strong and found in connective tissue

Hemoglobin

oxygen-binding protein of red blood cells that moves iron and oxygen around; a globular protein

Sickle-Cell Disease

change in primary structure; a substitution of amino acid (valine) not glutamic acid in the protein hemoglobin causing cells to deform and clog blood vessels

Determiners of Conformation Proteins

chemical and physical conditions of the proteins environment: temperature, pH, etc.

Denaturation

a protein unravels and loses its native conformation(shape) causing proteins to be biologically inactive

The Protein Folding Problem

most proteins go through several intermediate states on their way to a stable conformation; denatured proteins no longer work in their unfolded conditions

Chaperonins

protein molecules that assist in the proper folding of other proteins

X-ray crystallography

used to determine a proteins three-dimensional structure

Nucleic Acids

Stores and transmits hereditary information

Genes

the units of inheritance that program the amino acid sequences of polypeptides; they are made of nucleotide sequences on DNA

2 types of nucleic acids

deoxyribonucleic acid and ribonucleic acid

Deoxyribonucleic Acid (DNA)

found in the nucleus of the cell, DNA stores information for the synthesis of specific proteins; DNA is inherited from parents; it is encoded with info that programs cell's activities but does not directly run the operation of a cell

Chromosome

contains one long DNA molecule that consists 100 to 1000 genes

tools for biological functions

proteins are the molecular hardware of the cell

DNA Function

directs RNA synthesis (transcription), directs protein synthesis through RNA (translation)

Flow of genetic information

DNA -> RNA -> protein

Ribosomes

cellular structures of actual sites of protein synthesis

mRNA

messenger RNA moves instructions for creating proteins from the nucleus to the cytoplasm.

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