Diversity of Life, Molecules, and Membranes Flashcards
Emergent Properties
New levels of organization provide new functions.
Order of Organization
Domain->Kingdom->Phylum->Class->Order->Family->Genus->Species
Examples of Unity and Diversity
Diversity: obvious. Unity: DNA Codes, cilia
Macromolecules
Polymers built from monomers
Enzymes; give an example
Facilitate reactions. E.g: Sucrase breaking down sucrose
Dehydration and Hydrolysis; which break and which create?
Make: Dehydration. Break: Hydrolysis
Glucose Molecular Formula
C6H12O6
4 Types of Polysaccharides
Starch, Glycogen, Cellulose, Chitin
Starch (Function, Used by)
Storage, plants
Glycogen (Function, Shape, Used by)
Storage, branched hydrocarbons, animals
Cellulose (Function, Shape, Used by)
Structure, long strings, plant walls
Chitin (Function, Used by)
Structure, fungi and animal exoskeletons
Fats (Structure; 2 parts)
Glycerol and Fatty Acid
Saturated Fatty Acid
Saturated Hydrogens, no cis or trans
Unsaturated Fatty Acid
Cis or Trans bonding causes kinks that unsaturated the triglycerides.
Good, the Bad, the Ugly(really Bad) (Fatty acids)
Unsaturated Fats, Saturated Fats, Trans Fats
Fats: Function
Storage, Protection, Insulation
Why are Trans Fats Bad?
They increase levels of LDL cholesterol.
Phospholipids(Structure)
Hydrophilic head, and Hydrophobic double tail (fatty acids)
Proteins(monomer and polymer)
Amino acid monomers, polyPEPTIDE polymers via peptide bonds
Proteins (General use in cell)[1]
They are the TOOLS of the cell
Amino acid structure
Amino group, R group that provides function, and a carboxylic acid allowing formation of peptide bonds with Amino group
Polypeptides( 2 termini)
contains an amino terminus and a carboxy terminus
Proteins (Primary Structure)
Polypeptides
Proteins (2 Secondary Structures, and how they are bonded)
Alpha helices and Beta sheets created from hydrogen bonds
Proteins (Tertiary Structure causes)[5 interactions]
Interactions between R groups. [Hydrogen bonding, Disulfide bridges, Ionic Bonds, Van Der Waals, and hydro (phobic/philic) exclusions.]
Factors that affect enzyme function
Temperature, pH
Lipids (3 functions)
Hormones, Energy, Cell membranes
Sterols (Steroids)(3 properties, and structure)
Are hormones, largely hydrophobic, used in membrane structure [cholesterol], 4 RING STRUCTURES
Lipoprotein Complex
Transport for hydrophobic molecules such as cholesterol. Made of phospholipid ball, apoproteins, and cholesterol.
Apo Proteins
Proteins involved in the lipoprotein complex
Good and Bad Lipoproteins
Bad: LDL(low density lip…), Good: HDL (high density lip…)
LDL and why it’s bad in large quantities
carries cholesterol from liver to body cells, can cause plaque buildup
HDL
picks up excess cholesterol from cells and delivers back to liver for disposal/recycling
Phospholipids (2 structures)
Phospholipid bilayer; micelles
4 pieces of a biomembrane
Phospholipid bilayer, proteins, cholesterol, oligosaccharides
Function of Cholesterol in Membrane
Gives rigid strength to membrane
Oligosaccharides (Where and functions (2))
3-10 monomer polysaccharides attached to membrane proteins and phospholipids. Helps with marker/ID, and connect to cytoskeleton.
Factors that affect membrane fluidity(3)
Temperature, phospholipids, steroids
How does temperature affect membrane fluidity?
Higher temperature: melting, denaturation
Lower temperature: less fluid/permeable–>solidification
What phospholipid characteristics alter membrane fluidity?
Saturated: less fluid/permeable
Unsaturated: more fluid/permeable
What steroid characteristics alter membrane fluidity?
More cholesterol can increase strength of membrane, but decrease fluidity
Glycoprotein
a protein with a carbohydrate attached
Types of Transport[General] (2)
Passive Transport and Active Transport
Types of Passive Transport (3)
Simple Diffusion, Facilitated Diffusion, Osmosis
Simple Diffusion (2 facts)
High to low concentration, movement of small uncharged hydrophobic molecules such as estrogen and testosterone, or GASES
Facilitated Diffusion is aided by what kinds of proteins?
Transmembrane channel proteins and Carrier Proteins
Channel Proteins (4 facts)
Sometimes gated, requiring a SPECIFIC signal, rapid response, for small molecules
Carrier Proteins
Changes shape, for larger molecules, e.g: glucose transporters
Osmosis
Movement of water down the gradient, no energy investment
Osmosis Channel Proteins are called….
Aquaporins, involved for fast water transfer
If the solution a cell is in is HYPERtonic, which way does water move, and what happens to the cell?
If solution is HYPERtonic, water moves from higher concentration IN CELL TO lower concentration OUTSIDE OF CELL. This causes the cell to SHRINK.
If the solution a cell is in is HYPOtonic, which way does water move, and what happens to the cell?
If solution is HYPOtonic, water moves from higher concentration OUT OF CELL TO lower concentration INSIDE OF CELL. This causes the cell to BURST.
Active Transport (2 facts)
movement against gradient, needs energy
Energy process for Active Transport
ATP (Adenisone TRIphosphate) undergoes hydrolysis and loses a phosphate group to mechanism. Comes out as ADP (Adenisone Diphosphate)
Active Transport Types (2)
Protein pumps, and Bulk Transport
Transmembrane Pumps
Can be very specific proteins that use ATP to change shape, releasing one ion and capturing another into cell.
Bulk Transport (Vesicular Transport)(3 types)
Phagocytosis, Pinocytosis, Receptor mediated endocytosis
Phagocytosis
LARGE food particles engulfed by membrane
Pinocytosis
Bringing in SMALLER RANDOM particle pockets and picking and choosing.
Receptor Mediated Endocytosis and example with LDL
Very selective receptors exist on membrane, waiting for specific particles to hit the membrane. E.g : LDL Receptors that bind to apoproteins on LDL lipoprotein complex. Receptors reused.
