Biology Flashcards
When did life on Earth begin?
Approximately 3.5-4 billion years ago.
What are the levels of biological organization?
- atoms
- molecules and macromolecules
- cells
- tissues
- organs
- organism
- population
- community
- ecosystem
- biosphere
natural selection
when a mutation causes a beneficial change in survival or reproduction and the frequency of that mutation increases across generations
Prokaryote
simple cell structure
- bacteria
- archaea
eukaryote
Larger cells with internal compartments that serve various functions. Cells have a nucleus
- protists
- plants
- fungi
- animals
What are the taxonomic levels?
- Domain
- Kingdom
- Phylum
- Class
- Order
- Family
- Genus
- Species
genome
complete genetic composition of an organism
proteome
all of the proteins that a cell or organism can make
theory
broad explanation of some aspect of the natural world that is substantiated by a large body of evidence
What are the types of particles within atoms?
- protons (in atomic nucleus)
- neutrons (in atomic nucleus)
- electrons (in orbitals at various distance from the nucleus)
ion
atom that has gained or lost one or more electrons
valence electrons
electrons in the outermost shell of the atom
atomic number
given based on the number of protons the element has
isotopes
elements that differ in the number of neutrons
radioisotopes
unstable isotopes that persis for a long time and lose energy by emitting subatomic particles and/or radiation
What elements are living organisms mainly made of?
- oxygen
- carbon
- hydrogen
- nitrogen
trace element
present in extremely small quantity but is essential for normal growth/function
-example: iron
covalent bond
atoms share electrons
- can occur between atoms whose outer shells are not full
- strong bonds
polar covalent bond
one atom is more electronegative that the other and shared electrons create poles with one atom more negative than the other
nonpolar covalent bond
bond between atoms with similar electronegativities
hydrogen bond
hydrogen atom from one polar molecule becomes electrically attracted to the electronegative atom in another polar molecule
-weak on their own but strong if there’s enough of them (ex: in DNA)
van der Waals forces
short-lived electrical attraction due to unevenly distributed electrons in orbit
ionic bond
bond between negative and positive ions
-bond easily broken in water
cation
ion with net positive charge (lost and electron)
anion
ion with net negative charge (gained electron)
chemical reaction
one or more substances are changed into other substances
-requires energy (usually heat)
Brownian motion
heat energy causing atoms and molecules to vibrate/move
catalyst
substance that speeds up a chemical reaction
-ex: enzyme
What are the properties of water?
- ions and polar molecules readily dissolve in water
- water is a polar covalent bond
- high specific heat - amount of heat needed to raise temperature
- cohesion - water molecules attract to each other (hydrogen bonds)
- adhesion - water attracted to and adheres to a surface that is not electrically neutral
organic molecule
carbon-containing molecule
-lipids, carbs, proteins, nucleic acids
urea
natural organic product formed from the breakdown of proteins in an animals body
How many covalent bonds can carbon form?
4
- 4 electrons in outer shell, wants 8 total
- can form non-polar and polar covalent bonds
isomers
2 structures with an identical molecular formula but different structures and characteristics
What are carbohydrates used for in the body?
They are used for energy! To make ATP!
They circulate blood into cells. Inside cells, enzymes break down glucose into smaller molecules. This releases energy stored in the bonds that are breaking down. This new energy is then stored in the bonds of ATP.
polysaccharides
“many sugars”
- starch, glycogen
- used to store energy in cells
- can be broken down to sugars, which can be broken down to make ATP
Are lipids hydrophilic or hydrophobic?
Hydrophobic!
How are fats (triglycerides) formed?
Bonding glycerol to 3 fatty acids
fatty acid
a chain of carbon and hydrogen atoms with a carboxyl group (-COOH) at one end
saturated fatty acid
all carbon in the fatty acid are linked by single covalent bonds. They can pack together tightly
unsaturated fatty acid
At least one of the carbon bonds are linked by a double covalent bond. unsaturated fatty acids cannot pack together tightly
What are fats used for?
They store energy. Hydrolysis of triglycerides releases the fatty acids from glycerol. The fatty acids can be metabolized to provide energy to make ATP
phospholipid
The third hydroxyl group of glycerol is linked to a phosphate group instead of a fatty acid. This makes one end polar/hydrophilic and the other end is hydrophobic. This causes them to be organized into bilayers
-cell membranes
steroid
- lipid with a skeleton that has 4 fused rings of carbon atoms
- different than other types of lipids
- cholesterol is converted to other steroids by modifying side groups
- one or more hydroxyl groups are attached to the ring structure, but not enough to make a steroid water soluble
What elements are proteins made of? What are the building blocks of proteins?
- made of C, H, O, N, and small amounts of other elements (sulfer)
- polymers of amino acids
peptide bond
covalent bond formed between a carboxyl and amino group
polypeptide
many amino acids joined by peptide bonds
protein
1+ polypeptides that have been folded and twisted into a certain 3D shape to do a particular function
protein primary structure
amino acid sequence in straight line
protein secondary structure
amino acid sequence is folded into more complex structure
protein tertiary structure
polypeptide folds and refolds upon itself to assume a 3D shape
protein quaternary structure
2+ polypeptides of tertiary structure assembled with each other
-ex: hemoglobin (4 protein subunits)
nucleic acids
responsible for the storage, expression, and transmission of genetic info
-polymers that are made of neucleotides
What are the building blocks of nucleic acids?
Nucleotides
What are the two classes of nucleic acids?
- deoxyribonucleic acid (DNA)
- riboneucleic acid (RNA)
DNA
stores genetic info coded in the sequence of their monomer building blocks (nucleotides)
RNA
involved in decoding DNA info into instructions for linking specific sequence of amino acids to form a polypeptide chain
What are the bases (nucleotides) of DNA?
purine bases -adenine -guanine pyrimidine bases -cytosine -thymine
What are the bases (nucleotides) of RNA?
purine bases -adenine -guanine pyrimidine bases -cytosine -uracil
prokaryote
- simple cell structure
- lack a mambrane-enclosed nucleus
- bacteria and archaea
plasma membrane
double layer of phospholipids and embedded proteins
-barrier between cell and external environment
cytoplasm
region of cell contained within the plasma membrane
ribosome
involved in polypeptide synthesis
cell wall
relatively rigid structure that protects plasma membrane and cytoplasm
-porous
organelle
membrane-bound compartment with its own unique structure and function
nucleus
where most of DNA is housed
cytosol
outside the organelles but inside the plasma membrane. The fluid in the cytoplasm.
-metabolism occurs here
metabolism
sum of chemical reactions by which cells produce the materials and utilize the energy necessary to sustain life
catabolism
breakdown of molecules into smaller components
anabolism
synthesis of cellular molecules and macromolecules
cytoskeleton
network of 3 types of protein filaments (microtubles, intermediate filaments, actin filaments)
-provides cell shape, organization, and movement
motor proteins
proteins that use ATP as a source of energy to promote movement
-interact with cytoskeletal filaments to promote movement
nuclear envelope
double-membrane structure that encloses the nucleus
nuclear pores
provide passageway for movement of molecules/macromolecules into/out of nucleus
chromosome
composed of DNA and proteins that help to compact the chromosome to fit in nucleus
chromatin
chromosome-protein complex
What is the function of the nucleus?
protect, organize, replicate, express DNA
-assemply of ribosome subunits
nucleolus
where the assembly of ribosom subunits occurs
rough endoplasmic reticulum
key rold in sorting proteins that are destined for the endoplasmic reticulum, Golgi apparatus, lysosomes, vacuoles, plasma membrane, or outside of the cell
smooth endoplasmic reticulum
provides increases surface area for key enzymes that play important metabolic roles
- enzymes in smooth ER are critical in synthesis and modifications of lipids (estrogen and T production)
- sit of detoxification
Golgi apparatus
- processing and modifying certain proteins and lipids
- protein sorting
- secretion of materials (package of materials into secretory vesicles that later fuse with the plasma membrane to release contents)
lysosome
small organelles in animal cells that lyse/break macromolecules
vacuoles
temporarily store or transport materials in animal cells
peroxisomes
catalyze the breakdown of harmful molecules
What are the characteristics of the cell membrane?
- semi-permeable (plasma membrane proteins transport nutrients, ions, etc. into-out of cell
- cell signaling (cell membrane receptors get signals (environmental, hormones) that triggers cell to have a response
- cell adhesion (proteins on mombranes can allow cells to interact)
semiautonomous organelles
can grow and divide to reproduce themselves
- mitochondria and chloroplasts (plants only)
- have their own DNA
- divide by binary fission (splitting in 2)
mitochondrian
site where ATP is made
- convert chemical energy stored within covalent bonds of organic molecules into a form (ATP) that can be readily used by cells
- involved in synthesis, modification, breakdown of several types of molecules (synthesis of certain hormones)
- have their own DNA
- divide by binary fission (splitting in 2)
protein sorting signals
short stretches of amino acid sequences on proteins that direct them to their correct cellular location
protein cotranslational sorting
translation at ribosome halts until ribosome binds to the endoplasmic reticulum membrane
-translation resumes and protein is sorted by ER
protein post-translational sorting
sorting does not occur until translation is finished
What are the primary components of cell membranes?
- phospholipids
- proteins embedded or attached to membrane
- carbs (lesser component)
Described the phospholipid bilayer (polarity etc.)
- hydrophilic (polar) head on surface
- hydrophobic (nonpolar) tails on interior
- because of hydrophobic interior, membrane is a barrier to movement of ions and hydrophilic molecules
Why is the phospholipid bilayer semi-fluid?
- it’s short tails are less likely to interact with each other (makes them more fluid)
- fatty acid tail are unsaturated fats (have double bond) which make membrane more fluid and makes interactions more difficult
- cholesterol is present and is rigid
How does the cholesterol in the plasma membrane make it more or less fluid with changing temperature?
- at higher temperature, cholesterol makes membrane less fluid
- at lower temperature, cholesterol makes membrane more fluid (prevents freezing)
What is the advantage of plasma membrane being semi-permeable?
ensures essential molecules enter cell, metabolic intermediates remain in cell, waste products exit cell
diffusion
sustance moves from region of higher concentration to region of lower concentration
-passive transport
facilitated diffusion
transport proteins provides a passageway for the substance to cross the plasma membrane
-passive transport
passive transport
transport of a substance across a membrane from a region of high concentration to low concentration
-does not require input of energy
active transport
moves substance from an area of LOW concentration to HIGH concentration (against a concentration gradient) with the aid of a transport protein
-requires the input of energy (ATP hydrolysis)
isotonic
solute concentrations on both sides of membrane are equal
hypertonic
solute concentration is higher on this side of membrane compared to other side
hypotonic
solute concentration on this side of membrane is lower than other side
osmosis
water diffuses acress membrane from hypotonic compartment to hypertonic compartment
-when solutes cant readily move across membrane
primary active transport
type of transport that directly uses energy to transport solute against a gradient
secondary active transport
use of a pre-existing gradient to drive the active transport of another solute
-Na+/K+ pump (Na+/K+ ATPase)
exocytosis
material inside cell is packaged into vesicles and excreted into extracellular environment
-for transport of very large molecules (proteins, polysaccharides)
endocytosis
plasma membrane invaginates to form a vesicle that brings substances into cell
-for very large molecules (proteins, polysaccharides)
enzyme
proteins that act as critical catalysts to speed up different reactions in cells
-creat or breakdown reactions
metabolism
sum total of all chemical reactions that occur within an organism
- most create or breakdown molecules
- cells use intermediate molecules (ATP) to drive chemical reactions in a desired direction
energy
ability to producy change or do work
1st law of thermodynamics
energy cannot be created or destroyed
-can be transferred from one place to another or transferred between types of energy (i.e. chemical energy transferred to heat)
2nd law of thermodynamics
transfer of energy or transformation of energy from one form to another increases the entropy (degree of disorder) of a system
free energy
amount of available energy that can be used to promote change or do work
exergonic reaction
free energy is released during product formation
-spontaneous reaction
endergonic reaction
required addition of free energy
-NOT a spontaneous reaction (forms reactants)
hydrolysis of ATP
energy liberated is used to drive a variety of cellular processes
-ATP with addition of water breaks down to ADP + Pi (inorganic phosphate)
activation energy
initial input of energy to get molecules close enough to interact
- enzymes lower activation energy
- positions molecules closer together
enzyme inhibitors
bind to enzyme and inhibit their functions
competitive inhibitor
enzyme inhibitor that binds directly to active site so substrate can’t find it
noncompetitive inhibitor
enzyme inhibitor that binds noncovalently to an enzyme at a location outside the active site (an allosteric site) and inhibits the enzymes function
metabolic pathway
coordinated sequences of reactions
-each step catalyzed by a specific enzyme
catabolic reaction
breaks down molecules
- usually exergonic
- recycle organic building blocks and produce energy intermediates (ATP, NADH)
- can then use building blocks and energy intermediates to make new macromolecules
anabolic reaction
builds molecules
-usually endergonic and must be coupled to an exergonic reaction
glycolosis
breakdown of glucose to pyruvate
- catabolic reaction
- creates ATP
oxidation
removal of 1+ electrons from atom/molecule (oxygen frequently involved/receiving electron)
reduction
adds electron(s) to atom/molecule -reduces charge
redox reaction
one side is oxidized, other side is reduced
- electrons often go to NAD+ to make NADH
- NADH can be used to make ATP
- NADH also gives electrons to help anabolic reactions
cellular respiration
metabolic reactions that a cell uses to get energy from food molecules and release waste products
-makes ATP
aerobic respiration
uses oxygen to make ATP and releases CO2
- carbs, proteins, fats can be used as energy sources to drive respiration (glucose)
- glucose + 6O2 -> 6CO2 + 6H2O + energy intermediates (ATP) + heat
What are the pathway steps of aerobic respiration?
- glycolysis (glucose broken down into pyruvate, makes ATP)
- breakdown of pyruvate to an acetyl group in mitochondria (makes NADH)
- citric acid cycle in mitochondria (each acetyl group is incorporated into an organic molecule which is later oxidized to release CO2 (makes ATP, NADH, FADH2)
- oxidative phosphorylation (oxidation of NADH and FADH2 via electron transport chain provides more energy to make ATP, O2 is consumed, makes a lot of ATP. O2 is the final step of the electron transport chain to receive an electron, H2O is produced. At the end of electron transport chain, ATP synthase helps synthesizes ATP via oxidative phosphorylation)
anaerobic respiration
creates energy in the absence of sufficient oxygen (i.e. strenuous exercise). Has 2 different strategies:
- use a substance other than O2 as final electron acceptor in electron transport chain
- produce ATP only via substrate-level phosphorylation (an enzyme directly transfers a phosphate from an organic molecule to ADP)
How can glycolysis occur without O2
pyruvate from glycolysis is reduced to make lactate
- no net oxidation
- called fermentation
- yields WAY less ATP (2 vs ~30 during aerobic respiration)
direct intercellular signalling
- direct contact between cells
- junctions enable them to pass ions, signaling molecules, etc. to one another
contact dependent cell signaling
-membrane-bound signaling receptors allow molecules to be in contact with both cells
autocrine cell signaling
- cell secretes signaling molecules that bind to receptors on its own cell surface, stimulating a response
- can affect nearby cells of same cell type
paracrine cell signaling
cell secretes signals that affect nearby target cells (but not itself)
endocrine cell signaling
secretion of hormones into bloodstream that travel up to long distances to target cells
-longer lasting signaling
What are the steps of cell signaling response?
- receptor activation (signaling molecule binds to receptor, causing confirmational change that activates its function)
- signal transduction (activated receptor stimulates a series of proteins that forms a signal transduction pathways
- cellular response (signal transduction pathway affects the functions and/or amount of cellular proteins, thereby producing a cellular response)
transcription factors
proteins that regulate the transcription of genes
-ex: sex hormones do this
ligand
cell signaling molecule
-binds noncovalently to cell receptor with high specificity
enzyme-linked cell receptor
extracellular dowmain binds to signal (ligand), intracellular domain has a cataclytic function activated
G-protein-coupled cell receptor
when bound to signal (ligand), interacts with intracellular G proteins
- causes G protein to bind with GTP instead of GDP
- G protein dissociates into alpha and beta, which causes response
ligand-gated ion channel
ligand binds to receptor to open channel and allow flow of ions through membrane
intracellular receptor
located inside cell
- many steroid hormone receptors are intracellular
- hydrophobic hormones can pass through plasma membrane
- steroid hormones bind receptors in nucleus
What are the roles of extracellular matrix?
- strength
- structural support (bones)
- organization (propoer arrangement of cells, binds body parts)
- cell signaling
cell junctions
specials structures that link cells
- anchoring junctions (attach cells to each other and to the ECM)
- tight junctions (forms tight seal between cells to prevent material from leaking between cells)
- gap junctions (small gap occurs between the plasma membranes of cells connected by these junctions