Feralis Ch 1 Flashcards
Ionic Bonds
Transfer of electrons from one atom to another where both atoms have different electronegativities
Non-polar covalent bonds
Equal sharing of electrons between two atoms of identical electronegativity
Polar covalent bonds
Unequal sharing of electrons between two atoms of different electronegativities, results in dipole formation
Hydrogen bonds
Weak bond between molecules with a hydrogen attached to a highly electronegative atom and is attracted to a negative charge on another molecule (F, O or N)
5 Properties of water
Excellent solvent, high heat capacity, ice floats, cohesion/surface tension, adhesion
Excellent solvent - water property
Dipoles of H2O break up charged ionic molecules, making it easy for water to dissolve substances
High heat capacity - water property
Water requires large amount of energy to change the temperature degree. Water also has high heat of vaporization
Ice floats - water property
Water expands when frozen and becomes less dense than liquid water. This is because the H bonds become rigid and form crystal that keeps the molecules separated
Cohesion/surface tension - water property
Water can be attracted to like substances because of its H bonds. There is strong cohesion between H2O molecules, producing a high surface tension
Adhesion - water property
Water can also be attracted to unlike substances. Capillary action is the ability of a liquid to flow without external forces (ex. up a vertical paper)
Organic molecules
Made of carbon atoms. Macromolecules from monomers, monomers form polymers
Hydroxyl
OH functional group, polar, hydrophilic
Carboxyl
COOH functional group, polar, hydrophilic, weak acid
Amino
NH2 functional group, polar, hydrophilic, weak base
Phosphate
PO4(3-) functional group, polar, hydrophilic, acid
Carbonyl
C=O functional group, polar, hydrophilic. Incorporated into aldehyde and ketone
Aldehyde
H-C=O functional group, polar, hydrophilic
Ketone
R-C=O functional group, polar hydrophilic
Methyl
CH3 functional group, non-polar, hydrophobic
Monosaccharide
Single sugar molecule (ex. glucose and fructose)
Disaccharide
Two sugar molecules joined by glycosidic linkage (occurs via dehydration reaction) (ex. sucrose, lactose, maltose)
Polysaccharide
Series of connected monosaccharides; polymer. Bonds form via dehydration synthesis and breakdown via hydrolysis
Sucrose
Disaccharide, glucose + fructose
Lactose
Disaccharide, glucose + galactose
Maltose
Disaccharide, glucose + glucose
Carbohydrates
Includes sugars, starches and fibres. Composed of the “-saccharides”
Starch
A carbohydrate, a polymer of alpha-glucose molecules, stores energy in plant cells
Glycogen
A carbohydrate, a polymer of alpha-glucose molecules, stores energy in animal cells
Cellulose
A carbohydrate, a polymer of beta-glucose, structural molecules for walls of plant cells and wood
Chitin
A carbohydrate, a polymer similar to cellulose, but each beta-glucose group has a nitrogen containing group (n-acetylglucosamine) attached to the ring, it is structural molecule in fungal cells and insect cytoskeletons
Lipids
Hydrophobic, for insulation, energy storage, make up structural components like cholesterol and phospholipids in membranes, participates in endocrine signalling
Triglycerides (Triacylglycerols)
A lipid, 3 fatty acid chains attached to glycerol backbone, can be saturated or unsaturated
Saturated triglycerides
A lipid, no double bonds, has straight chains, bad for health because straight chains stack densely and form fat plaques
Unsaturated triglycerides
A lipid, contains double bonds that cause kinks, better for health because chains can stack less densely, can be cis or trans
Phospholipids
A lipid, composed of 2 fatty acids and a phosphate group (+R) attached to a glycerol backbone. It is amphipathic
Steroids
A lipid, composed of three 6-membered rings and one 5-membered ring, includes (sex) hormones, cholesterol, corticosteroids
Waxes
A lipid, esters of fatty acids and monohydroxylic alcohols, used as protective coating or exoskeletons (lanolin)
Carotenoids
A lipid, fatty acid carbon chains with conjugated double bonds and 6-membered C-rings at each end. Includes pigments that produce colours in plants and animals. Subgroups are carotenes (orange) and xanthophylls (yellow)
Porphyrins (tetrapyrroles)
A lipid, 4 joined pyrrole rings that often complex with a metal (ex. porphyrin heme complexes with Fe in hemoglobin; chlorophyll with magnesium)
Adipocytes
A lipid, specialized fat cells, two categories are white fat cells and brown fat cells
White fat cells
An adipocyte, a lipid, composed primarily of triglycerides with a small layer of cytoplasm around it
Brown fat cells
An adipocyte, a lipid, have considerable cytoplasm, lipid droplets scattered throughout, and lots of mitochondria
Glycolipids
A lipid, similar to phospholipids but have a carbohydrate group instead of phosphate group
Lipoproteins
A lipid, transports the insoluble lipids in the blood, are lipid cores surrounded by phospholipids and apolipoproteins
Cell membrane fluidity
Part of lipids, cell membranes need to maintain certain degree of fluidity and are capable of changing membrane fatty acid composition to do so
Cell membrane fluidity in cold weather
Cell membrane becomes more rigid. To avoid rigidity, cholesterol, monounsaturated and polyunsaturated fatty acids are incorporated into the membrane, which increases fluidity
Cell membrane fluidity in warm weather
Cell membrane becomes more fluid and flexible. To avoid cell membrane collapse, cholesterol is added to restrict movement. Fatty acid tails are saturated so they become straight and pack tightly, which decreases fluidity
Protein
Polymers of amino acids joined by peptide bonds. Have alpha-carbon attached to side chain, H, amino group and carboxyl group. Functions include structure, storage, transport, defence (antibodies) and enzymes. RNA can act as an enzyme sometimes (ex. ribozymes)
Storage proteins
casein in milk, ovalbumin in egg whites, zein in corn seeds
Transport proteins
Hemoglobin carries oxygen, cytochromes carry electrons
Enzymes
Catalyze reactions based on substrate concentration, does not change spontaneity of a reaction. Enzyme efficiency determined by temperature and pH. Amylase catalyzes reactions that breaks the alpha-glycosidic bonds in starch
Cofactors
Non-protein molecule that assists enzymes by donating or accepting some component of a reaction (such as electrons or functional groups), can be organic (called coenzyme, ex. vitamins) or inorganic (ex. metal ions like Fe2+ and Mg2+)
Holoenzyme
Union of cofactor and enzyme
Apoenzyme/Apoprotein
Enzyme is not combined with a cofactor
Coenzyme
Organic cofactor, ex. vitamins, usually donate or accept electrons
Prosthetic group
Cofactor binds tightly or covalently bound to an enzyme
Simple protein
Formed entirely of amino acids
Albumins and globulins
Functional proteins that act as carriers or enzymes
Scleroproteins
Fibrous proteins, have structural function (ex. collagen)
Conjugated proteins
Simple protein + non-protein
Lipoprotein
Protein bound to lipid
Mucoprotein
Protein bound to carbohydrate
Chromoprotein
Protein bound to pigmented molecule
Metalloprotein
Protein complexed around metal ion
Nucleoprotein
Contains histone or protamine, bound to nucleic acid
Primary protein structure
Sequence of amino acids connected by peptide bonds
Secondary protein structure
3D shape resulting from hydrogen bonding between amino and carboxyl groups of adjacent amino acids (alpha helix or beta sheet). Hydrogen bonds, disulfide bonds and Van Der Waals forces
Tertiary protein structure
3D folding pattern resulting from non-covalent interactions between amino acid R groups (side chain interaction). Non-covalent interactions include H bonds, ionic bonds, hydrophobic effect (R groups push away from water), disulfide bonds, and Van Der Waals forces
Quaternary protein structure
3D shape of a protein that is a grouping of 2 or more separate peptide chains
Protein structure
All proteins have primary structure, most have secondary structure, larger proteins may have tertiary and quaternary structure.
3 main protein categories
Globular proteins, fibrous/structural proteins and membrane proteins
Globular proteins
A protein category, somewhat water soluble, mostly dominated by tertiary structure, diverse range of functions including: enzymatic, hormonal, intercellular and intracellular storage and transport, osmotic regulation, immune response
Fibrous/structural proteins
A protein category, not water soluble, mostly dominated by secondary structure, made of long polymers, function to maintain and add strength to cellular and matrix structure (ex. collagen or keratin)
Membrane protein
A protein category, includes proteins that function as membrane pumps, channels or receptors
Protein denaturation
Protein is reversed back to primary structure, usually irreversible. Denaturation may be reversed with removal of denaturing agent. Implies that all information needed for a protein to assume its native state (its folded functional form) is encoded in its primary structure
Protein denaturation vs protein digestion
Denaturation reverses protein to primary structure. Digestion eliminates all protein structure, including the primary structure
Nucleotides
Monomers that make up nucleic acids and consist of a nitrogenous base, a 5-carbon deoxyribose sugar and a phosphate group.
Nucleosides
Sugar and nitrogenous base
Nitrogenous base
Nitrogen-containing compound that makes up a nucleotide and can vary based on DNA or RNA.
Nitrogenous bases of DNA
A and T pair with 2 H bonds. C and G pair with 3 H bonds
Nitrogenous bases of RNA
A and U (uridine) pair with 2 H bonds. C and G pair with 3 H bonds
Pyrimidines
1 ring, cytosine, uracil, thymine
Purines
2 rings, adenine, guanine
DNA
Deoxyribose sugar, 2 antiparallel strands of a double helix
RNA
Ribose sugar, single stranded
Cell theory
i. All living organisms are composed of one or more cells ii. The cell is the basic unit of structure, function, and organization in all organisms iii. All cells come from preexisting, living cells iv. Cells carry hereditary information
RNA world hypothesis
Proposes that self-replicating RNA molecules were precursors to current life. States that RNA stores genetic information (similar to DNA) and catalyzes chemical
reactions (similar to enzyme). RNA may have played a major role in the evolution of cellular life. RNA is unstable, compared to DNA, due to its extra hydroxyl group that makes it more likely to participate in chemical reactions!
Central dogma of genetics
Information must travel from DNA -> RNA -> protein
Ranking Biological Scale
Relative sizes of different cell elements at structures
Stereomicroscope (light)
Uses visible light to view the surface of a sample.
Pro: can view living samples
Con: has low light resolution compared to a compound microscope
Compound Microscope (light)
Uses visible light to view a thin section of a sample.
Pro: can view some living samples (single cell layer)
Con: may require staining for good visibility
Phase Contrast Microscope
Uses light phases and contrast for a detailed observation of living organisms, including internal structures.
Pro: has good resolution and contrast
Con: not ideal for thick samples and produces a “Halo Effect” around perimeter of samples
Confocal Laser Scanning Microscope and Fluorescence
Used to observe thin slices while keeping a sample in tact; common method for viewing chromosomes during mitosis
Pro: can observe specific parts of a cell using fluorescent tagging
Con: can cause artifacts
Note: confocal laser scanning microscopes can be used without fluorescence as well, in which laser light is used to scan a dyed specimen and display the image digitally
Scanning Electron Microscope (SEM)
Pro: view surface of 3D objects with high resolution
Cons: can’t use on living samples, preparation is extensive as sample needs to be dried and coated, is costly
Cryo Scanning Electron Microscope (Cryo SEM)
Pro: sample is not dehydrated so you can observe samples in their more ‘natural form’
Cons: can’t use on living samples, samples must be frozen, which can cause artifacts
Transmission Electron Microscope (TEM)
Pros: can observe very thin cross- sections in high detail, and can observe internal structures with very high resolution
Cons: cannot be used on living samples, preparation of sample is extensive, and technique is costly
Electron Tomography
not a type of microscope, but a technique used to build up a 3D model of sample using TEM data
Pro: can look at objects in 3D and see objects relative to one another
Cons: cannot be used on living samples, preparation of sample is extensive, and technique is costly
Centrifugation
Common technique used to prepare a sample for observation or further experimentation. It spins and separates liquified cell homogenates into layers based on density.
Order of pellet in centrifugation
Cell parts separate with the most dense pelleting first and least dense separating last. We spin and extract the dense pellet, and spin again and repeat. In cells, starting from first component to pellet at the bottom and progressively spinning faster, the order is: nuclei layer -> mitochondria/ chloroplasts/lysosomes → microsomes/small vesicles → ribosomes/viruses/larger macromolecules
Differential centrifugation
Relies on density, shape, and speed at which macromolecule travels
Density centrifugation
Based on density, separates cell parts within the same pellet group created from differential centrifugation. Forms continuous layers of sediment: insoluble proteins can be found in the pellet, soluble proteins remain in the supernatant liquid above the pellet.
Reaction at equilibrium
The rate of formation of reactants and products is equal and there is 0 net production.
Anabolic reactions
Chemical reactions in which small molecules are assembled into larger molecules
Catabolic reactions
Chemical reactions in which large molecules are broken down into small molecules
Catalysts
Enzymes, lowers activation energy of a reaction, accelerates the rate of the overall reaction, enzymes are substrate specific, enzymes remain unchanged during reaction, catalyzes both forward and reverse directions of the reaction, varying function based on pH and temperature, has an active site that binds substrates via induced fit
ATP
Common source of activation energy, stores its potential energy in the form of chemical energy, formed via phosphorylation, ADP and Pi come together using energy from an energy rich molecule like glucose.
Allosteric enzymes
Enzyme that has both an active site for substrate binding and an allosteric site for the binding of an allosteric effector (can be an activator or inhibitor)
Competitive inhibition
A substance that mimics the substrate and inhibits the enzyme by binding at the active site. The effect of competitive inhibition can be overcome by increasing substrate concentration
Uncompetitive / anti-competitive inhibition
Occurs when an enzyme inhibitor binds only to the formed enzyme-substrate (ES) complex (and not to the free enzyme), preventing formation of product. Vmax and Km are lowered
Vmax
Maximum velocity of the enzyme
Km, Michaelis constant
Represents the substrate concentration at which the rate of reaction is half of Vmax.
Relationship between Km and binding affinity
Inverse relationship; higher Km equals worse
substrate binding, lower Km equals better substrate binding.
i. A small Km indicates that an enzyme only requires a small amount of substrate to become saturated. Hence, Vmax is reached at relatively low substrate concentrations.
ii. A large Km indicates the need for high substrate concentrations to achieve Vmax.
Cooperativity
Phenomenon that occurs where an enzyme becomes more receptive to additional substrate molecules after one substrate molecule binds to the active site
i. Example: hemoglobin is a quaternary protein with 4 subunits that each has an active site for binding oxygen. As the first oxygen binds, the other active sites become increasingly likely to bind oxygen.
ii. Note: hemoglobin is not an enzyme, but is used here as a simple example of biological cooperativity that you will encounter later.
8 types of membrane proteins
Channel proteins, recognition proteins, ion channels, porins, carrier proteins, transport proteins, adhesion proteins, receptor proteins
Channel proteins
A type of membrane protein, provide a passageway through the membrane for hydrophilic (water-soluble), polar, and charged substances
Recognition proteins
A type of membrane protein, type of glycoprotein (have an attached oligosaccharide) that is used to distinguish between self and foreign (e.g major-histocompatibility complex on macrophage)
Ion channels
A type of membrane protein, used to pass ions across the membrane and referred to as gated channels in nerve and muscle cells
i. Can be voltage-gated (respond to
difference in membrane protein), ligand-gated (chemical binds to open channel), or mechanically-gated (respond to pressure, vibration, pressure)
Porins
A type of membrane protein, allows the passage of certain ions and small polar molecules; increase the rate of water passing in kidney and plant root cells; tend to be less specific - if you can fit through the large passage, you can go through
Carrier proteins
A type of membrane protein, specific to movement across the membrane via integral membrane protein; changes shape after binding to specific molecule that enables it to be passed across (e.g glucose into the cell)
Transport proteins
A type of membrane protein, includes active transport that uses ATP (e.g sodium-potassium pump) and facilitated diffusion that does not use ATP
Adhesion proteins
A type of membrane protein, attach cells to neighboring cells and provide anchors for stability via internal filaments and tubules
Receptor proteins
A type of membrane protein, serve as binding sites for hormones and other trigger molecules
3 membrane properties
Phospholipid membrane permeability, cholesterol, glycocalyx
Phospholipid membrane permeability
A type of membrane property, allows small, uncharged, non-polar, hydrophobic molecules to freely pass the membrane. Polar molecules may cross if they are small and uncharged. Every other type of substance requires a transporter
Cholesterol
A type of membrane property, adds rigidity to animal cell membranes under normal conditions and maintains fluidity of the membrane at lower temperatures; sterols provide analogous function in plant cells
Note: prokaryotes do not have cholesterol in their membranes - use hopanoids instead
Glycocalyx
A type of membrane property, a carbohydrate coat that covers the outer face of the cell wall of some bacteria and the outer face of the plasma membrane in some animal cells; consists of glycolipids attached to the plasma membrane, and glycoproteins that may serve as recognition proteins. Functions include adhesive capabilities, barrier to infection, or markers for cell-cell recognition
Peripheral membrane proteins
Generally hydrophilic and are held in place by H- bonding and electrostatic interactions. Can disrupt/ detach them by changing salt concentration or pH
Integral proteins
Hydrophobic, can be destroyed using detergent
Chromatin
General packaging structure of DNA around proteins in eukaryotes; tightness in packaging depends on cell stage
Chromosomes
Tightly condensed chromatin when the cell is ready to divide
Histones
DNA coils around it into bundles called nucleosomes; these bundles are wrapped around 8 histone proteins
Nucleosomes
DNA coiled around 8 histone proteins
Nucleolus
Inside of the nucleus and serves as the site of ribosome synthesis
Ribosome synthesis
Synthesized using rRNA and ribosomal proteins, which are imported from the cytoplasm. Once ribosomal subunits form, they are exported to the cytoplasm for final assembly into a complete ribosome.
Nucleus
Bound by proteins like RNA polymerase and histones. There is no cytoplasm in the nucleus, there is nucleoplasm. Found only in eukaryotic cells, not in prokaryotic cells
Nuclear Lamina
Dense fibrillar network inside of the nucleus of eukaryotic cells that provides mechanical support; helps regulate DNA replication, cell division, and chromatin organization