Bio: Biological Macromolecules

a. Carbohydrates(starch) b. Lipid(triacylglycerol) c. Protein(enzyme) d. Nucleic acid(DNA)

• All living things are made up of these four classes of biological molecules

• within cells, small organic molecules are joined together to form larger molecules

Macromolecules

• are large molecules composed of thousands of covalently connected atoms

Monomers

• the small building-block molecules to make a polymer

Polymer

• a long molecule consisting of many similar building blocks

Dehydration reaction/ Condensation reaction

• occurs when two monomer bond together through the loss of a water molecule

Hydrolysis

• process of disassembling polymers to monomers

• a reaction that is essentially the reverse of the dehydration reaction

Enzyme

• are macromolecules that speed up the dehydration process

Carbohydrate

• include sugars and the polymers of sugars

Monosaccharides

• also known as simple sugars, the simplest carbohydrates

Polysaccharides

• are carbohydrate macromolecules

• these are polymers composed of many sugar building blocks

Sugars

what carbohydrate has monosaccharides that have molecular formulas that are usually multiples of CH20

Glucose(C6H12O6)

• the most common monosaccharide

Carbonyl group

1. Aldose

2. Ketose

• what is highlighted?

1. functions as an aldehyde

2. functions as a ketone

Disaccharide

• formed when a dehydration reaction joins two monosaccharides

Glycosidic linkage

• the covalent bond that forms disaccharides

Maltose • Glucose & Glucose

• disaccharide used in brewing • give the two monosaccharides bonded

Lactose • Glucose & Galactose

• disaccharide used in transporting the sugar in milk • give the two monosaccharides bonded

Sucrose • Glucose & Fructose

• disaccharide used in transporting sugar in plants • give the two monosaccharides bonded

Polysaccharides

• the polymers of sugars, have storage and structural rolls that are determined by its sugar monomers and the positions of glycosidic linkages

Starch • amylose & amylopectin

• a storage polysaccharide of plants, consisting entirely of glucose monomers

• stored in plants as granules within chloroplasts and other plastids • give the glucose monomers

Glycogen

• a storage polysaccharide in animals

• stored mainly in liver and muscle cells of humans and other vertebrates

Cellulose

• a structural polysaccharide that is a major component of the tough wall of plant cells

Chitin

• a structural polysaccharide found in the exoskeleton of arthropods

• it also provides structural support for the cell walls of many fungi

a. Monosaccharide b. Disaccharide c. Oligosaccharide d. Polysaccharide

(c) more than 2 (d) more than 100

Simple carbohydrates

• also known as sugars, are maid up of shorter chains of molecules and are quicker to digest than complex carbohydrates

Complex carbohydrates

• raises blood glucose levels for longer and produce a more lasting elevation in energy

• provides the body with energy better

Fiber

• a type of carbohydrate that the body can’t digest

Lipids

• the one class of large biological molecules that do not form polymers

• are hydrophobic because they consist mostly of hydrocarbons which form non-polar covalent bonds

Fats

• lipids that are constructed from 2 types of smaller molecules: glycerol and fatty acids

• separates from water because water molecules form hydrogen bonds with each other and exclude the fats

• its major function is energy storage

1. Glycerol

2. Fatty Acid

(1) a three-carbon alcohol with a hydroxyl group attached to each carbon (2) consists of carboxyl group attached to a long carbon skeleton; varies in length(number of carbons) and in the number and locations of double bonds

1. Ester linkage

2. Triacylglycerol/triglyceride

(1) joins three fatty acids to glycerol (2) results of (1)

1. Carboxyl group

2. Hydroxyl group

Saturated fatty acids

• fatty acids that have the maximum number of hydrogen atoms possible and NO double bonds

• solid at room temperature

• what most animal fats are

Unsaturated fatty acids

• fatty acids that have one or more double bonds

• liquid at room temperature

• what plant fat and fish fat are

a. Cis fat b. Trans fat

• indicate the configuration of the molecule around the double bond (a) if hydrogen are present in the same plane; causes bending (b) if the hydrogen atoms are on 2 different planes

Phospholipids

• where 2 fatty acids and a phosphate group are attached to glycerol

• the major component of all cell membranes

Phospholipid bilayer a. hydrophobic b. hydrophilic

• result from the structure of phospholipids found in cell membranes (a) the 2 fatty acid tails in a phospholipid; points toward the interior when phospholipids are added to water (b) the phosphate group in a phospholipid and its attachment

Steroids

• lipids characterized by a carbon skeleton consisting of four fused rings

Cholesterol

• an important steroid, is a component in animal cell membranes

• essential in animals but high levels in blood may contribute to cardiovascular disease

Cortisol

• a steroid hormone that when released, raised your cholesterol level

a. cortisol b. corticosterone c. aldosterone d. progesterone e. Beta-estradiol f. testosterone

Glycolipids

• a type of complex lipids comprising carbohydrates, fatty acids, sphingolipids or a glycerol group

• mainly describe any compound containing one or more monosaccharides residues bound by glycosidic linkage

• found on the leaflet of cellular membranes

• maintains membrane stability & facilitates cell-cell communication

Proteins • Hemoglobin

• account for more than 50% of the dry mass of most cells • give the protein that helps in the transfer of oxygen in blood

Enzymatic proteins

Function: selective acceleration of chemical reactions Example: Digestive ________ catalyze the hydrolysis of bonds in food molecules

Storage proteins

Function: Storage of amino acids Examples: CASEIN, the protein of milk, is the major source of amino acids for baby mammals. Plants have storage proteins in their seeds. OVALBUIM is the protein of egg white

Defensive proteins

Function: protection against disease Example: Antibodies inactivate and help destroy viruses and bacteria

Transport proteins

Function: transport of substances Example: HEMOGLOBIN, the iron-containing protein of vertebrate blood, transports oxygen from the lungs to other parts of the body

Hormonal proteins

Function: coordination of an organism’s activities Example: INSULIN, a hormone secreted by the pancreas, causes other tissues to take up glucose, thus regulating blood sugar concentration

Receptor protein

Function: response of cell to chemical stimuli Example: receptors built into the membrane of a nerve cell detect signaling molecules released by other nerve cells

Structural proteins

Function: support Examples: KERATIN is the protein of hair, horns, feather and other skin appendages. COLLAGEN and ELASTIN proteins provide a fibrous framework in animal connective tissues

Contractile & motor proteins

Functions: movement Examples: Motor proteins are responsible for the undulations of cilia and flagella ACTIN and MYOSIN proteins are responsible for the contraction of muscles

Gene Regulatory proteins

• Bind to DNA in particular locations and determine whether or not certain genes will be read.

• Allows cell to becomes specialized for different functions and respond to changes in their surroundings

Sensory proteins

• detect environmental changes like light and respond by emitting or producing signals that call for a response

a. Amino acids b. Polypeptide c. Protein

(a) Are organic molecules with carboxyl and amino groups (b) polymers built from the same set of 20 amino acids (c) consist of one or more polypeptides

Amino group

R groups

• the differing chains that differ the properties of amino acids

Glycine (Gly/G)

• nonpolar side chains; hydrophobic

Alanine (Ala/A)

• nonpolar side chains; hydrophobic

Valine (Val/V)

• nonpolar side chains; hydrophobic

Leucine (Leu/L)

• nonpolar side chains; hydrophobic

Isoleucine (Ile/I)

• nonpolar side chains; hydrophobic

Methionine (Met/M)

• nonpolar side chains; hydrophobic

Phenylalanine (Phe/F)

• nonpolar side chains; hydrophobic

Tryptophan (Trp/W)

• nonpolar side chains; hydrophobic

Proline (Pro/P)

• nonpolar side chains; hydrophobic

Serine (Ser/S)

• polar side chains; hydrophilic

Threonine (Thr/T)

• polar side chains; hydrophilic

Cysteine (Cys/C)

• polar side chains; hydrophilic

Tyrosine (Tyr/Y)

• polar side chains; hydrophilic

Asparagine (Asn/N)

• polar side chains; hydrophilic

Glutamine (Gln/Q)

• polar side chains; hydrophilic

Asparitic acid (Asp/D)

• electrically charged side chains; hydrophilic

• Acidic(negatively charged)

Glutamic acid (Glu/E)

• electrically charged side chains; hydrophilic

• Acidic(negatively charged)

Lysine (Lys/K)

• electrically charged side chains; hydrophilic

• Basic (positively charged)

Arginine (Arg/R)

• electrically charged side chains; hydrophilic

• Basic (positively charged)

Histidine (His/H)

• electrically charged side chains; hydrophilic

• Basic (positively charged)

Peptide bonds

• links amino acids

Polypeptide

• a polymer of amino acids

• range in length from a few to more than a thousand monomers

• has a unique linear sequence of amino acids

a. Amino end b. Carboxyl end

Primary structure

• the sequence of amino acids in a protein, is like the order of letter in a long word

• determined by inherited genetic information

Secondary Structure a. Alpha helix b. Beta-pleated sheets

• its coils and folds result from hydrogen bond between repeating constituents of the polypeptide backbone (a) a coil structure (b) folded structure

Tertiary structure

• determined by interactions between R groups, rather than interaction between backbone constituents

Hydrogen bond

• can form between the different amino acids

Disulfide bridge

• can form between 2 cysteine side chains

• are strong covalent bonds that may reinforce the protein’s structure

Ionic bond

• can form between groups with opposite charge

van der Waals attraction

• weak attractions between atoms due to oppositely polarized electron clouds

Hydrophobic exclusion

• the tendency of the multiple oil droplets that are present in water to coalesce into fewer and larger droplets.

Quaternary structure

• results when 2 or more polypeptide chains form one macromolecule

Denaturation

• altercations in secondary to quaternary structure without altering the primary structure

• the loss of a protein’s naive structure due to alterations in pH, salt concentration, temperature or other environmental factors

• this kind of protein is biologically inactive

Chaperonins

• are protein molecules that assist the proper folding of other proteins

X-ray crystallography

• determines a protein’s structure

Nuclear magnetic resonance(NMR) spectroscopy

• determines a protein’s structure which does not require protein crystallization

Bioinformatics

• uses computer programs to predict protein structure from amino acid sequences

Gene

• a unit of inheritance that programs the amino acid sequence of a polypeptide

• made of DNA

Deoxyribonucleic acid (DNA)

• type of nucleic acid

• provides directions for its own replication

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

Ribonucleic acid (RNA)

• type of nucleic acid

Protein synthesis • Transcription • Translation

• occurs in the ribosomes; has 2 stages

1. DNA is copied to RNA

2. RNA is used to produce proteins

Polynucleotides

• polymers of nucleic acids