Biology DAT Ch. 1-5 Flashcards
Matter
Anything that takes up space and has mass
Element
Purest substance that has physical/chemical properties, cannot be broken down
Atom
Smallest unit of matter with chemical properties
Molecule
one or two atoms joined together
Intramolecular forces
attractive forces holding atoms within a molecule
Intermolecular forces
forces that exist between molecules & affect physical properties of the substance
Monomers
single molecules that can be polymerized
Polymers
substance made up of monomers
Carbohydrates
Carbon, hydrogen, and oxygen (CHO). Come in forms of monosaccharides, disaccharides, and polysaccharides
Monosaccarides
carbohydrate monomers with the empirical formula (CH2O)n. n indicating the number of carbons.
Ribose
5 carbon monosaccarides
Fructose
6 carbon monosaccarides
Glucose
6 carbon monosaccarides
Disaccharides
Two monomers joined together by a glycosidic bond. This bonds is created by dehydration reaction.
Dehydration (condensation) reaction
Water molecule leaving, thus covalent bond is formed
Hydrolysis reaction
Water molecule added and covalent bond is broken
Sucrose
glucose + fructose
Lactose
galactose + glucose
Maltose
glucose + glucose
Starch
energy storage for plants and is a (alpha) bonded polysaccharides.
Glycogen
energy storage for humans and is a (alpha) bonded polysaccharide. Is much more branched than starch.
Amylose
linear starch
Amylopectin
branched starch
Cellulose
structural component of plant cell well, its b (beta) bonded polysaccharides. Linear strands are packed rigidly in parallel.
Chitin
component of fungi cell wall and insect exoskeleton, bonded by b (beta) polysaccharides, with nitrogen added to each monomer
Polysaccharides
multiple monomers bonded by glycosidic bonds in a long polymer
Proteins
contain hydrogen, carbon, oxygen, and nitrogen (CHON). These combine to form amino acids, which link up to form polypeptides.
Polypeptides
(proteins) polymers of amino acids linked by peptide bonds through dehydration and hydrolysis reactions. It forms an amino acid chain with two end terminals on opposite sides.
Amino acids
20 different, each have a different R-group
N-terminus
(amino terminus) the polypeptides side that ends with the last amino acid’s amino group
C-terminus
(carboxyl terminus) the polypeptide side that ends with the last amino acid’s carboxyl group
Protein structure
primary, secondary, tertiary, and quaternary structure
Protein classification
globular, fibrous, intermediate
Protein denaturation
temperature change, pH change, and salt concentration
Protein functions
storage immunity receptors enzymes hormones motion structure
Protein composition
conjugated (amino acids + other components) and simple (amino acids)
Primary structure
sequence of amino acids
Secondary structure
alpha and beta pleated sheets formed by hydrogen bonding due to intermolecular forces between polypeptide backbone
Tertiary structure
3D structure due to interactions between R-groups. Hydrophobic and hydrophilic. Disulfide bonds are created by covalent bonding between R-groups of two cysteine amino acids.
Quaternary structure
multiple polypeptides chains coming together to form one protein
Storage
reserve of amino acids
Hormones
provide signaling throughout the body to regulate physiological processes
Receptors
Proteins in cell membrane which bond to signal molecules to trigger changes inside the cell
Motion
movement generated for a cells or of an entire organism
Structure
Provide strength and support to tissues
Immunity
Prevention and protection against foreign invaders
Enzymes
acts as a biological catalyst, binding to the substrate (reactants) to convert them into products
Catalyst
increases reaction rate by lowering activation energy, it reduces energy in the transition state. They do not shift chemical reaction & do not affect spontaneity
Transition State
unstable intermediate between reactants and products
Active site
site on enzyme where substrate binds, it is specific
Specificity constant
measures how efficient the substrate binds with the enzyme and converting it to a product
Induced fit theory
the active site changes shape to fit the substrate when it binds, also known as “lock and key” model
Ribozyme
RNA molecule that acts as an enzyme
Cofactor
non-protein molecule that helps enzymes perform its reaction
Coenzyme
An organic cofactor such as vitamins. (inorganic=metal ions)
Holoenzymes
cofactor + enzyme
Apoenzymes
enzyme + NO cofactor
Prosthetic groups
cofactor tightly or covalently bonded with its enzyme
Competitive inhibition
competitive inhibitor competes with substrate for the active site binding. Adding more substrate would increase enzyme reaction rate.
Km = increases
Vmax = stays the same
Noncompetitive inhibition
noncompetitive inhibitor does not compete for active site but instead binds on allosteric site, thus modifying the active site. Adding more substrate would NOT increase enzyme reaction rate.
Km = stays the same
Vmax = decreases
Allosteric site
other site on enzyme that is not the active site
Enzyme kinetics plot
can be used to visualize how inhibitors affect enzymes
Michaelis Constant (Km)
substrate concentration at which velocity is 50% of vmax
Vmax
maximum reaction of velocity
Saturation
occurs when all active sites are occupied, so the rate of reaction does not increase anymore despite increasing substrate concentration
Lipids
Carbon, hydrogen, and oxygen (CHO), they have long hydrocarbon tails making them very hydrophobic
Triacyglycerol
a lipid molecule with a glycerol backbone and 3 fatty acids linked by ester linkages
Ester linkages
links glycerol back bone and the 3 fatty acids
Glycerol backbone
3 carbon and 3 hydroxyl groups
Saturated fatty acids
no double bonds and as a result pack TIGHTLY (solid at room temperature)
Unsaturated fatty acids
double bonds by monounsaturated fatty acids and polyunsaturated fatty acids
Cis-Unsaturated fatty acids
have kinks that cause the hydrocarbon tails to bend, thus do not pack tightly
Trans-Unsaturated fatty acids
have straighter hydrocarbon tails so they pack more tightly (unhealthy)
Phospholipids
lipid molecule that have glycerol backbone, one phosphate group, and 2 fatty acids, causing it to be amphipathic, thus spontaneously assembling into a lipid bilayer
Cholesterol
lipid molecule that has 4 fused hydrocarbon rings. It is amphipathic. It is the most common precursor to steroid hormones. It helps with membrane fluidity
Steroid hormones
cholesterol is its precursor, 4 hydrocarbon rings
Cholesterol is starting material
material for vitamin D and bile acids
Membrane fluidity
temperature: increase of temp = increase of fluidity
cholesterol = holds membrane together at HIGH temp and keeps membrane fluid at LOW temp
degree of unsaturation
Lipoproteins
allow the transportation of lipid molecules into the blood stream due to out coat of phospholipids, cholesterol, and proteins
Low-Density Lipoproteins (LDLs)
“Bad Cholesterol”
low protein density, delivers cholesterol to peripheral tissues, and vessel blockage can occur
High-Density Lipoproteins (HDLs)
“Good Cholesterol”
high protein density, delivers and takes cholesterol away from peripheral tissues to the liver to make bile (reduces blood lipid levels)
Waxes
Hydrophobic protective coating, simple lipids that have long fatty acids connected to monohydroxy alcohols through ester linkages
Carotenoids
Pigments, lipid derivatives containing long carbon chains with conjugated double bonds and 6 membered rings at each end.
Nucleic acids
Carbon, hydrogen, oxygen, nitrogen, and phosphorus (CHONP). Nucleotide monomers that build into DNA or RNA polymers.
Nucelosides vs Nucleotides
Nucleoside
- ribose sugar and nitrogenous base
Nucleotide
- ribose sugar, nitrogenous base, and phosphate group
Deoxyribose sugar
contain hydrogen at the 2’ carbon
Ribose sugar
contain hydroxyl group at the 2’ carbon
Purines
A, G (two rings)
Pyrimidines
C T and U (one ring)
Phosphodiester bonds
connect the phosphate group of one nucleotide at the 5’ carbon to the hydroxyl group at the 3’ carbon. A series of phosphodiester bonds create the sugar-phosphate backbone with a 5’end free phosphate and a 3’end free hydroxyl.
Nucleic acids polymerizaion
proceeds as nucleoside triphosphate are added to the 3’ end of the sugar-phosphate backbone
DNA
double stranded, antiparallel double helix, two complementary strands with opposite directionalities (5’ and 3’ end) twist around each other.
RNA
single stranded after being copied from DNA during transcription, U replaces T and binds to A.
Modern Cell Theory
- All lifeforms have one or more cells.
- The cell is the basic structural, functional, and organizational unit of life.
- All cells from from other cells (cell division).
- Genetic information is stored and passed down through DNA
- An organism’s activity is dependent on the total activity of its independent cells.
- Metabolism and biochemistry (energy flow) occurs within cells
- All cells have the same chemical composition within organisms of similar species.
Central Dogma of Genetics
information is passed through DNA –> RNA –> Protein
exceptions: reverse transcriptase and prions
RNA world hypothesis
states that RNA dominated Earth’s primordial soup before there was life. RNA developed self-replicating mechanisms and later could catalyze reactions such as protein synthesis to make more complex macromolecules. Since RNA is reactive and unstable, DNA later became way of reliably of storing genetic information.
A-T bond
2 hydrogen bonds
G-C bond
3 hydrogen bonds
Cell membrane
is made up of phospholipids, cholesterol, and proteins
Membrane proteins
are either integral or peripheral membrane proteins
Integral (transmembrane) proteins
Transverse the entire bilayer, thus it is amphipathic. Assist in transport and cell signaling.
Peripheral membrane proteins
is found outside the bilayer, thus it is hydrophilic. Assist with cell recognition, receptor, adhesion.
Receptor
Trigger secondary responses within cell for signaling
Adhesion
attaches cells to other things (e.g. other cells).
Cellular recognition
proteins which have carbohydrate chains (glycoproteins). Used by cells to recognize other cells.
Glycoproteins
any of a class of proteins that have carbohydrate groups attached to the polypeptide chain. They form hydrogen bonds with the water molecules surrounding the cell and thus help to stabilize membrane structure.
Fluid Mosaic Model
describes how the components that make up the cell membrane can move freely within the membrane (fluid). Thus, the cell membrane contains many different kinds of structures (mosaic).
3 types of transport across the cell membrane
Simple diffusion, facilitated diffusion, and active transport.
Simple diffusion
flow of small, uncharged non-polar substances (e.g. O2 and Co2) across the cell membrane from high to low without using energy.
Osmosis
simple diffusion that involved water molecules
Facilitated transport
integral proteins allow larger, hydrophilic molecules to cross the cell membrane; uniporters, symporters, or antiporters, channel proteins, carrier proteins, passive diffusion, porins and ion channels
Channel proteins
Integral protein open tunnel from both sides of bilayer
Carrier proteins
Integral protein that binds to a molecule on one side to change the shape to bring it to the other side
Passive diffusion
performed by channel proteins,, bring molecules down their concentration gradient without energy use (similar to simple diffusion but a protein channel is used). E.g. porins and ion channels
Active transport
substances that travel against their concentration gradient and require the consumption of energy by carrier proteins.
Sodium-potassium pump
us a primary active transport that uses ATP hydrolysis to pump molecules against their concentration gradient. It establishes membrane potential.
Secondary active transport
uses free energy released when other molecules flow down their concentration gradient (gradient established by primary active transport) to pump the molecule of interest across the membrane.
Cytosis
refers to the bulk transport of large, hydrophilic molecules across the cell membrane and requires energy (active transport mechanism).
Endocytosis
cell membrane wrapping around an extracellular substance, internalizing it into the cell via vesicle or vacuole. Phagocytosis, pinocytosis, and receptor-mediated endocytosis.
Phagocytosis
cellular eating around solid objects
Pinocytosis
cellular drinking around dissolved materials (liquids)
Receptor-mediated endocytosis
requires binding of dissolved molecules to peripheral membrane receptor proteins, which initiates endocytosis.
peripheral membrane receptor proteins
initiates endocytosis, binds to dissolved molecules for receptor-mediated endocytosis
Exocytosis
opposite of endocytosis, releasing material to the extracellular environment through vesicle secretion
Organelles
cellular compartments enclosed by phospholipids bilayers (membrane bound) located in the cytosol.
Cytosol
aqueous intracellular fluid
Cytoplasm
cytosol + organelles
Prokaryotes
do not have organelles but have other adaptation such as keeping their genetic material in a region called the nucleoid.
Nucleus
primarily functions to protect and house DNA. DNA replication and transcription occurs here (DNA –> mRNA).
Nucleoplasm
is the cytoplasm of the nucleus
Nuclear envelope
membrane of the nucleus. Two phospholipids bilayers (outer and inner) with a perinuclear space in the middle
Nuclear pores
holes in the nuclear envelope that allows molecules to travel in and out of the nucleus
Nuclear lamina
provides structural support for the nucleus, as well as regulating DNA and cell division
Nucleolus
is a dense area that is responsible for making rRNA, and producing ribosomal subunits.
ribosomal subunits
rRNA + proteins
Ribosomes
not an organelle but work as small factories that carry out translation (mRNA –> protein). Composed of ribosomal subunits.
Eukaryotic ribosomal subunits
(60s + 40s) to assemble in the nucleoplasm and form a complete ribosome in the cytosol of 80s.
Prokaryotic ribosomal subunits
(50s + 30s) to assemble in the nucleoid and form the complete ribosome in the cytosol 70s.
Free-floating ribosomes
ribosomes make proteins that function in the cytosol
Rough ER
ribosomes make proteins that are sent out of the cell or to the cell membrane. Rough ER is continuous with the outer membrane of the nuclear envelope. Proteins synthesized by the embedded ribosomes are sent into the lumen for modifications (glycosylation).
Smooth ER
Not continuous. Its main function is to synthesize lipids, detoxify cells, and produce steroid hormones.
Golgi apparatus
made up of cisternae (flattened sacs) that modify and package substances. Vesicles come from the ER and reach the cis face of the Golgi and leave from the trans face.
Lysosomes
membrane-bound organelles that break down substances taking through endocytosis. They contain acidic digestive enzymes that function at low pH. They carry out autophagy and apoptosis.
Autophagy
breakdown of the cell’s own machinery for recycling
Apoptosis
programmed cell death
Transport vacuoles
transport material between organelles
Food vacuoles
temporarily hold endocytosed food and later fuse with lysosomes
Central vacuoles
large in plants and have a specialized membrane called tonoplast that helps maintain cell rigidity by exerting turgor. Functions in storage and material breakdown.
Storage vacuoles
stores pigments, starches, and toxic substances