CellMolTest1

• All organisms are composed of one or more cells
• The cell is the structural unit of life
• Cells arise from pre-existing cells by division (aren't spontaneously created)

• Life
• Highly complex and organized
• Posses a genetic program and the means to use it
• Capable of producing more of themselves
• Aquire and utilize energy
• Carry out a variety of chemical reactions
• Engage in mechanical activities
• Able to respond to stimuli
• Capable of self regulation
• Evolve over time

• Mycoplasma: smallest known cells
• Cyanobacteria: photosynthetic, gave rise to green plants and O2 rich atmosphere
• Some capable of N2 fixation

• Methanogens
• Halophiles
• Acidophiles
• Thermophiles

• E. Coli (bacterium)
• Saccharmyces (yeast)
• Arabidopsis (mustard plant)
• C. elegans (nematode)
• Drosophila (fruit fly)
• M. musculus (mouse)

• Embryonic stem cells have more potential for differentiation than adult stem cells (pluripotent). Must be differentiated in vitro.
• Cell repl therapy: somatic cell + denucleated egg = cells that won't be rejected by host
• Induced pluripotent cells: reprogramming of fully differentiated cel into pluripotent stem cell

• Volume of cytoplasm that can be effectively controlled by the genes in the nucleus
• Volume of cytoplasm that can be supported by exchange of nutrients
• Distance over which substances can efficiently diffuse

Virion

• Lytic: virus redirects host into making more particles then lyses to release viruses
• Integration (lysogenic): virus integrates its DNA into host's chromosomes. May give rise to progeny via budding, may become cancerous, may cause lysis after triggered event

Pathogens that consist ONLY of a single naked RNA molecule that binds to single stranded mRNA making them unreadable by ribosomes

• Absence of intermediate stage of evolution
• Symbiotic relationships seen amongst other organisms
• Organelles contain their own DNA, arrange prokyaryotically
• rRNA sequencing reveals similar structure of eu organelles and pro
• Organelles duplicate independently of nucleus

Water + energy = cleaving of polymers

• (CH2O)n
• Ketose sugars: Carbonyl (c=o) on terminal carbon
• Aldose sugars: Carbonyl on terminal carbon
• Enantiomers: D or L. D is found in nature.
• Glycosidic bonds (H-O-H)
• Glycogen, Starch, Cellulose, Chitin, Glycosaminoglycans (cell/cell communication).

• C attached to amine, carboxyl, H, and R group
• L stereoisomer (opposite of sugar)
• Peptide bonds

• Primary: sequence of amino acids
• secondary: conformation of adjacent amino acids in a-helix or b-sheet
• tertiary: conformation of entire polymer
• quaternary: protein subunits interacting
• multiprotein complex

Creutzfeld-Jakob Disease, Mad dow, kuru, scrapie. Prion (misfolded protein) causes other proteins to fold abnormally.

• Study of the proteome (entire inventory of organism's proteins)
• Current technology can create artificial genese to code for specific AA sequences

• Pentose (5-cardbon) sugar [ribose or deoxyribose]
• Phosphate group
• Nitrogenous base

• Purines: Adenine, Guanine
• Pyrimidines: Cytosine, Thymine, Uracil

• 1) Law of conservation of energy: Energy can neither be created nor destroyed, it is tranduced between states
• Change in internal E = heat - work (deltaE = Q - W), dE neg is exothermic, dE pos is endothermic
• 2) Events in universe tend to proceed from higher E to lower E. Loss of available E during the process is result of tendency for entropy of universe to increase. (TdeltaS)

• dH = dG + TdS (aka dG = dH - TdS). dG neg means rxn is spontaneous (exergonic), dG pos means rxn is endergonic
• At equilibrium dG = 0 (no free energy)
• Correction for standard conditions dG = dGstandard + RT lnK

• Cofactor: inorganic enzyme conjugates (metals)
• Coenzymes: organic enzyme conjugates (vitamins)
• Typically located within the active site of an enzyme

• Substrate orientation
• Changes in substrate reactivity
• Inducing strain in substrate
• Conformational changes

• Vmax = velocity at saturation
• Turnover # = number of substrate -> product per minute per enzyme molecule at Vmax
• Km (Michaelis constant) = substrate concentration at half Vmax (reflects affinity of enzyme for substand. Lower Km indicates higher affinity for enzyme)

• Irreversible inhibitors: bind tightly to the enzyme
• Reversible inhibitors: bind loosely to the enzyme
• -competitive inhibitors: compete w/ enzyme for active sites (can be overcome w/ increased substrate)
• -noncompetitive inhibitors: bind to alternate sites, change shape of enzyme (Vmax cannot be reached, inhibition cannot be overcome)

NAHD is oxidized to NAD+ by reducing pyruvate (lactate or ethanol)

Phosphate transfered to NAD+ from ATP when cell has much excess energy. NADPH is used for forming biomolecules, NADH allows the cell to create additional ATP.

• Compartmentalization
• Scaffold for biochemical activites
• Selectively permeable barrier
• Transporting solutes
• Responding to external signals
• Intercellular interaction
• Energy transduction

• Phosphoglycerides (diacylglycerides w/ small functional head groups)
• Sphingolipids (sphingosine to fatty acids)
• Cholesterol (smaller, less amphipathic, only animals)

spontaneous lipid bilayer that occurs in aqeuous environments

• Glycoproteins are for interactions with other cells/outside cell
• Glycolipids may be cell-to-cell recognition sites

• Integral: aphipathic, anchored in in the bilayer and hydrophilic regions. Anchored to one side (eg channel proteins)
• Peripheral: easy to removed, attached by weak bonds
• Lipid-anchored: Glycophophatidylinsoitol (GPI)-linked found on outer leaflet, weak bonds

• Simple diffusion: small, nonpolar
• Open channels: (ion channels, v-gated channels) ions
• Facilitated Diffusion: large, hydrophilic. Use of cotransport
• Active transport (pumps): 3Na out, 2K in