Water might be the most amazing molecule on Earth and it can defy gravity
Water molecule
Two elements of hydrogen for every element of oxygen form with polar covalent bonds
Water molecule
Oxygen has a partial negative charge while each hydrogen atom has a partial positive charge
This uneven distribution of charge results in a polar molecule
Hydrogen bonding
Forms between a partial positive hydrogen of one water molecule and a partial negative oxygen of another water molecule
Properties of water
Adhesion
Cohesion
Surface tension
Water movement in plants
1. Adhesion to plant vasculature walls
2. Cohesion between water molecules
3. Transpiration at leaves creates a pulling force
Matter is made up of atoms, has mass and takes up space
Energy is not made up of atoms
Atoms
Contain protons, neutrons and electrons
Metabolism
The sum of all chemical reactions that take place within an organism, including bond-breaking catabolic reactions and bond-forming anabolic reactions
Organic molecules
Contain carbon, which forms four covalent bonds
Six most common elements in living things
Carbon
Hydrogen
Nitrogen
Oxygen
Phosphorus
Sulfur
Dehydration reaction
Used to join monomers together and form a larger polymer, by removing water
Hydrolysis reaction
Adds water to break a polymer into monomers
Amino acid
Made up of one central carbon atom that forms four single covalent bonds, including to an acidic carboxyl group and a basic amino group, and a unique R group side chain
Protein synthesis
1. Amino acids link together through dehydration synthesis to form a polypeptide chain
2. The polypeptide chain undergoes further processing in the ER and Golgi body
Protein structure
Primary (amino acid sequence)
Secondary (alpha helix or beta sheet)
Tertiary (3D shape)
Quaternary (multiple polypeptide chains)
Protein denaturation
Disruption of hydrogen bonds that maintain protein structure, affecting function
Functions of proteins
Cellular membranes
Transport
Recognition
Movement
Communication
Tertiary structure
Specific 3D shape when alpha helices and beta sheets fold further inwards due to hydrogen bonding interactions
Quaternary structure
Two or more separate amino acid chains interacting and bonding together
Protein structure
Dependent upon the chemical properties of the R Group and can be influenced by environmental factors
Hydrophilic/charged R groups
Fold outward toward the aqueous environment
Hydrophobic R groups
Face the interior of the protein
Protein denaturation
Hydrogen bonds are disrupted, causing a change in shape that affects function, can sometimes be reversed
Roles of proteins in cells
Key component in cellular membranes
Transport
Recognition
Movement
Communication
Integral membrane proteins
Have hydrophobic regions that interact with phospholipid tails and hydrophilic regions adjacent to heads
Integral membrane proteins with channels
Have specific molecular chemistry internally forming a channel that may be gated and allow specific ions or small molecules to cross the membrane through facilitated diffusion or active transport
Peripheral proteins
More loosely attached to the membrane, involved in cell recognition and communication
Membrane proteins
Can provide anchorage for the cytoskeleton, aiding in structural support and cellular movement
Enzymes
Catalyze chemical reactions for specific substrates, have a specific active site that fits the substrate
Carbohydrates
Contain carbon, hydrogen and oxygen in a 1:2:1 ratio, formed from monosaccharide monomers joined by glycosidic bonds
Monosaccharides
Glucose, fructose, galactose
Disaccharides
Lactose, sucrose
Polysaccharides
Cellulose, chitin, starch, glycogen
Carbohydrate functions
Primary source of chemical energy, structural material
Glucose
C6H12O6, used in cellular respiration and photosynthesis
Lipids
Hydrophobic molecules with a H:O ratio greater than 2:1, include fats, phospholipids, steroids
Fats
Contain glycerol and long hydrocarbon fatty acid chains
Saturated fatty acids
Hydrocarbon chains with all single bonds, straight and closely packed