Bio

Bio unit one

Properties of water

adhesion, cohesion, high specific heat capacity, high specific heat vaporization, hydrogen bonding and density

Adhesion purpose

water molecules form H-bonds with other polar molecules, capillary action, makes polar substances souble

Cohesion

Water molecules form H-bonds with each other, high surface tension

High specific heat capacity

Large quantities of water are able to be absorbed by water without a significant change in its temperature, allowing organisms to maintain body temperature

High specific heat vaporization

Liquid water can absorb large amounts of energy to become a gas, allows an organism to rid heat by sweating.

Hydrogen bonding and density

H-bonds keep molecules spread out to reduce its density in solid form, allows ice to float

Weak acids

Don’t fully dissociate, are reversible, and allows the blood to remain at 7.35-7.45 pH

Properties of carbon

• Can form four bonds

• Can bind in chains, rings or branched structures

• molecules with C-H bonds are hydrocarbons

• Can form double or triple bonds

Functional groups

Branched groups of a hydrocarbon consisting of atoms other than hydrogen or carbon, they can make a molecule polar, ionic, soluble, or insoluble or acidic or basic

Buffers

Chemical that compensates for changes in pH by absorbing or releasing hydrogen

Monosaccharide

Simplest form of a sugar, categorized by number of carbons, have polar functional groups hydrophilic and water-soluble. Exist in linear form but fold when in water

Disaccharide

two monosaccharides in a DEHYDRATION reaction, becomes a glycosidic bond

Polysaccharide

100s of 1000s of monosaccharides linked. Provides energy storage and structural support

Polysaccharide characteristics

Highly polar, hydrophobic, too big to dissolve in water.

Types of polysaccharides

• Starch (amylose): glucose storage in PLANTS

• Glycogen: glucose storage in ANIMALS

• Cellulose: fibres of plant cell wall

• Chitin: insect exoskeleton

Dehydration/ glycosidic bonds

Isomer

Molecules with the same chemical composition, but different arrangement of atoms

Macromolecules

Lots of subunits binding together and forming a chain

Polymerization

Chemical bonding of subunits

Monomer

Each individual subunit

polymer

String of chemically joined subunits

Lipids

CHO, non-polar, insoluble in water, form cell membranes, store energy, and act as hormones

Fatty acids

Carboxyl group attached to a long hydrocarbon chain, as length increases, solubility decreases

Fats

1-3 fatty acids bonded to a glycerol through dehydration synthesis. Stores 2X the amount of energy of carbohydrates

Phospholipids

2 fatty acid chains and a Phosphate group attached to a glycerine. Contains polar head and non-polar tail. makes up Bilayer of cell membrane

Steroids

Four fused carbon rings, has side groups to give unique properties, Ex. Cholesterol

Waxes

Long fatty acid chains connected to Alcohol or carbon ring group, nonpolar, hydrophobic, soft solid at room temp

Saturated Fats

Single bonds in fatty acid chains, usually animal fats, are more compact, causes build up of fat in blood vessels (bad)

Unsaturated Fats

At least one double bond, usually found in plant produce, liquids at room temp, important to diet (good)

Trans Fats

An unsaturated fat chemically forced to accept more hydrogen, causing it to behave like a saturated fat. Solid at room temp, used for frying.

Protein

One or more polypeptides. Polymer made of amino acid, long chain folded into 3D structure, most diverse and vital worker of the cell

Amino acid

Monomer of protein, join together in different combinations. The central carbon is attached to an amino group, carbonyl functional group, and an “R” group.

“R” group

A hydrogen atom or carbon chains and rings. Gives amino acid its functional properties

Peptides

Chains of amino acid. Amino acid monomers form covalent bonds by dehydration synthesis, the amino joins with the acid group. A nitrogen terminal end, and a carbon terminal end.

Polypeptide

50 or more amino acids

4 levels of protein structure

primary, secondary, tertiary, quaternary

Primary protein structure

Unique sequence of amino acids in a polypeptide chain, linear, almost limitless combinations.

Secondary protein structure

Primary structure of coils and bands, b-pleated or a-helix

Tertiary protein structure

“R” groups interact to create a 3D structure. Makes the protein functional

Quaternary protein structure

Two or more polypeptides come together. Polypeptides are bonded with the same intermolecular forces as a tertiary structure

Prosthetic groups

Non-protein components embedded in the structure to carry out a function. (Hemoglobin in blood cells)

Nucleic Acids definition

Instructions for the production of proteins

DNA – deoxyribonucleic acid (stores genetic info)

RNA – ribonucleic acid (single stranded nucleotide involved in protein synthesis)

Nucleotide

Monomer unit of nucleic acid, contains nitrogenous base, 5-carbon sugar and 1-3 phosphate groups

Nucleic acid creation

The polymer chain that is created by the dehydration reaction between phosphate group and hydroxyl

Nitrogenous bases

Pyrimidines

• Uracil (U) → only in RNA

• Thymine (T) → only in DNA

• Cytosine (C)

  Purines

• Adenine (A)

• Guanine (G)

  A-T: 2 H-bonds

  G-C: 3 H-bonds

DNA

Double-stranded molecule, deoxyribose, phosphate, 4 bases. Two nucleotides that run antiparallel

RNA

Single stranded molecule, ribose, phosphate and 4 bases. can take on thort, linear forms

Phosphodiester bonds

The link that creates the backbone of a nucleic acid chain. on C-3 and P-4

Enzymes

Biological catalysts that increase activation rate. About 4000 in a typical cell. They have an activation site specific to the shape of the substrate and tightly close after it bonds with the substrate

Enzyme example

Lactase – catalyzes the breakdown of lactose

Chymosin - Hydrolysis of casein protein in milk to produce cheese curds

Other enzymes – break starch into glucose and improve stain removal

Enzyme cofactors

Many enzymes require cofactors to help them function. A non-protein component of and ion or organic molecule.

1) Enzyme and substrate concentration

The reaction rate depends on the amount of enzyme available

as substrate increases → collision increases → higher rate of reaction. However, max amount of enzymes limits combinations with substrate.

2) Enzyme inhibitors

Competitive: inhibitor competes with the substrate for the activation site (reversible, inhibitor binds weakly)

Non-competitive: inhibitor binds to another location on the enzyme, deactivating it (irreversible, inhibitors permanently deactivate it)

3) allosteric regulation

• Natural regulator of enzyme activity (reversible)

• binds to enzymes to stimulate activity, causing it to