Tags & Description
Covalent Bonds
Sharing a pair of valence electrons Strong bond Ex: Water atom
Cation
Anion
Ionic bonds
Transfer of electrons Strength relies on environment (in the middle) Ex: Salts
Hydrogen bonds
When a hydrogen atom in one molecule is attracted to the electrostatic atom in another molecule Very weak Ex: Only hydrogen is involved
Properties of water
-cohesive behavior -ability to moderate temperature -doesn't change temperature too quickly -expansion upon freezing -versatility as a solvent
Lower than 7 pH
Acid
Higher than 7 pH
Basic
pH scale reason
The PH of an atom is the measure (the percent) of the amount of hydrogen or hydronium within the atom (chance) (acids have more hydrogen, basics less)
Adhesion
An attraction between molecules of different substances
Cohesion
Attraction between molecules of the same substance
Polar molecule
Molecule with an unequal distribution of charge, resulting in the molecule having a positive end and a negative end
Hydrophilic
Affinity for water (polar)
Hydrophobic
Non-affinity for water (non-polar)
Surface tension
Breaking the hydrogen bonds
Solvent
Doing the dissolving
Solute
What's being dissolved
Non-polar dissolves
Non-polar
Polar dissolves
Polar
A solvent and a solute make a
Solution
Monomers
Building blocks of polymers
Polymers
Made up of monomers
Condensation reaction
A chemical reaction in which two or more molecules combine to produce water or another simple molecule
Dehydration reaction
A chemical reaction in which molecules combine by removing water
Hydrolysis reaction
A chemical reaction that breaks apart a larger molecule by adding a molecule of water
Monosaccharides
Single sugar molecules (short term energy)
Disaccharides
Carbohydrates that are made up of two monosaccharides
Polysaccharides
Carbohydrates that are made up of more than two monosaccharides
Carbohydrates
Monosaccharides, disaccharides, polysaccharides
Lipids
Triglycerides, phospholipids, steroids
Carbon
Backbone of all living things, has four valence (and only needs four) making it neutral. Will make double, triple, quadruple bonds
Hydrocarbons
Molecules consisting of only carbon and hydrogen (fuel ex.)
Buffers
Substances that minimize changes in concentrations of H+ and OH- in a solution. Used all the time to resist changes that can be possibly fatal.
Substrate
What an enzyme acts on
Enzymes are ___ in a reaction
Not consumed
Activation energy and enzymes
Enzymes are the first push that the reaction needs. Enzymes hasten reactions that would occur naturally.
Active site of an enzyme
The region of an enzyme that attaches to a substrate
Temp and pH affect enzymes
Depends per enzyme- each has an optimal condition
Competitive inhibitors
Reduce the productivity of enzymes by blocking substrates from entering active sites
Non-competitive inhibitors
Bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective
Exergonic
Energy releasing
Endergonic
Energy taking
Activation energy
Energy needed to get something going
Chemical energy
Potential energy available for release in a chemical reaction
Free energy
Energy that is available to do work
Enzymes
-ase. Each is made for a specific action/purpose.
Catabolic
Breaking down
Anabolic
Building up
Proteins
Nutrients the body uses to build and maintain its cells and tissues (chains of amino acids)
Steroids
A type of lipid characterized by a carbon skeleton consisting of four rings with various functional groups attached
Phospholipids
A molecule that is a constituent of the inner bilayer of biological membranes, having a polar, hydrophilic head and a nonpolar, hydrophobic tail
Triglycerides
An energy-rich compound made up of a single molecule of glycerol and three molecules of fatty acid
Primary protein structure
Sequence of amino acids (held together through peptide bonds)
Secondary protein structure
Coiling or folding of a polypeptide due to hydrogen bonding between amino acids
Tertiary protein structure
3D folding pattern of a protein due to side chain interactions of amino acids (hydrogen bonds between polar side chains and ionic bonds between negatively and positively charged side chains)
Quaternary protein structure
2+ protein chains forming functional protein. A 'braided' chain of two or more entirely identical or entirely different polypeptide chains.
Protein denaturation
When proteins are subject to heat, acid or other conditions that disturb their stability; protein uncoils, loses its shape, and loses its function