Chemistry Flashcards
Chemistry
Structure of matter
Matter
Anything that takes up space and has mass
Chemical properties
Determine physiology at molecular and cellular levels
Protons
Positive charge, 1 mass unit
Neutrons
Neutral, 1 mass unit
Electrons
Negative charge, low mass
Atomic number
of protons
Nucleus
Contains protons and neutrons
Molecule
Two or more atoms joined by strong bonds
Compound
Two or more atoms of different elements joined by strong or weak bonds
Three major types of chemical bonds
Ionic, covalent, hydrogen
Ion
Atom with an electric charge
Cation
Electron donor
Anion
Electron acceptor
Ionic bond
Attractions between cations and anions
Covalent binds
Strong electrons involving shared electrons
Single covalent bond
Sharing one pair of electrons
Double covalent bond
Sharing two pairs of electrons
Triple covalent bond
Sharing three pairs of electrons
Hydrogen bonds
Weak polar bonds between adjacent molecules based on electrical attractions
Organic molecules
Contain H, C, and usually O
Organic molecules include
Carbohydrates, lipids, proteins, nucleic acids
Monosaccharides def
Simple sugars with three to seven carbon atoms
Monosaccharides ex
Glucose (6C)
Disaccharides
Two monosaccharides (sucrose, maltose)
Polysaccharides def
Polymers of many sugars
Polysaccharide ex
Glycogen, starch, cellulose
Glucose stored…
In liver, skeletal muscle
Lipids
Hydrophobic molecules such as fats, oils, and waxes
Fatty acids (saturated)
No double bonds in hydrocarbon tail
Fatty Acids (Unsaturated)
One or more double bonds in tail
Glycerides
Fatty acids attached to glycerol molecule
Triglycerides
Glycerol plus three fatty acids
Triglyceride: 3 functions
- Energy source
- Insulation
- Protection
Steroids (class of fat)
Cholesterol, sex hormones, steroid hormones
Phospholipids and glycolipids
Hydrophobic tails, hydrophilic heads
Structural lipids
Components of plasma membrane
Proteins
Most abundant and important organic molecules
Amino acids
20, monomers that combine to form proteins
Primary structure
Sequence of amino acids along polypeptide
Secondary structure
Hydrogen bonds form spirals or pleats
Tertiary structure
Coiling and folding produce 3D shape
Quaternary structure
Final protein complex produced by interacting polypeptide chains
Globular proteins
Soluble spheres with active functions; shape based on tertiary structure
Fibrous proteins
Structural sheets or strands; shape based on secondary or quaternary structure
7 major protein functions
Support, movement, transport, buffering, metabolic regulation, coordination + control, defense
Enzymes
Lower activation energy of chemical rxn
Nucleic acids
Large organic molecules found in nucleus
DNA
Determines genetics, directs protein synthesis, control enzyme production, controls metabolism
RNA
Coordinates intermediate steps in protein synthesis
Complementary strands
In DNA; double helix; hydrogen binds btwn opposing nitrogenous bases holds them together
Single chain
mRNA, tRNA, rRNA
Complementary base pairs
DNA: AT, CG
RNA: AU
ATP
Adenosine triphosphate
Phosphorylation
Process of adding a phosphate group to another molecule