Chapters 5-9 COPY Flashcards
Four Classes of Biological Molecules (Macromolecules)
- Carbohydrates
- Lipids
- Proteins
- Nucleic acids
- All considered polymers except lipids
Macromolecules
- Large molecules, complex
- Unique properties that arise from the orderly arrangement of their atoms
- Polymers=macromolecules
Polymer
- A long molecule consisting of many similar building blocks
- Building blocks= monomers
Enzymes
-Specialized molecules that speed up chemical reactions
Dehydration reaction (condensation)
- When two monomers bond together through the loss of a water molecule
- Catalytic reaction
Hydrolysis
- How polymers break apart
- Reverse of dehydration reaction (adds water)
- Metabolic reaction
Carbohydrates
- Fuel, building material, Carbon source, information (blood ABO)
- 25% of dry cell mass
- Sugars and polymers of sugars
- Simplest= monosaccharides (simple sugars)
- Polysaccharides= many sugars
Lactose Intolerance
- Lactase= enzyme
- W/o enzyme or lack of, lactose (sugar) cannot be broken down, ferments in large intestine
Chitin
-Creates exoskeleton of arthropods
Lipids
- 5% of dry cell mass
- Not a true polymer
- Required for membrane, energy, signaling, insulation
- Hydrophonic
- Types: fat, phospholipid, steroid
Fats
- Constructed from glycerol and fatty acids
- Fatty acid= carboxyl group attached to carbon skeleton
- Glycerol= three carbon alcohol w/ hydroxyl group attached to each carbon
- Glycerol connects to chain of fatty acids
- Triacylglycerol: 3 fatty acids joined by glycerol
Saturated Fats
- Solid at room temperature (high melting point)
- No double bond
- Bad for health
Unsaturated Fats
- Liquid at room temp (low melting point)
- Double bond
- Cis: packed poorly, low melting point (better for u)
- Trans: packed tightly, high melting point (bad for u)
Lipid Bilayer
- Makes cell membranes
- One end of phospholipid is polar, other non-polar
- Hydrophilic head, hydrophobic tail
Steroids
- Ring structure: four fused ring
- Percusor= cholesterol, essential for membrane signaling
- Too much= bad (atherosclerosis, build up in arteries)
- Vitamin D and hormone
Nucleic Acid
- 10% dry cell mass
- Store, transmit, and help express hereditary info
- Multiple NA= gene–> multiple gene= DNA
- Polynucleotide made of monomers called nucleotides
Pyrimidines
-Cytosine, Thymine, Uracil
Purines
-Adenine and Guanine
DNA Structure
- Nucleotides linked by phosphodiester linkage
- Phosphate group that links two sugars
- Sequence of bases along a DNA or mRNA= unique to each gene
- Double helix
- A w/ T, G w/ C
- gene–> dna–> chromosome
RNA
-Single-stranded
Thymine is replaced by Uracil, so U and A pair
-More variable in form
Proteins
- 50% of dry mass of most cells
- Speed up chemical reactions, defense, storage, transport, cellular communication, movement, and structural support
Enzymatic Proteins
-Accelerate chem reactions
Defensive proteins
-Protection against disease
Storage proteins
-Store amino acids
Transport Proteins
-Transport of substances
Hormonal Proteins
-Ex: insulin
Receptor proteins
-Response of cell to chemical stimuli
Contractile and motor proteins
-Movement
Structural proteins
-Support
Polypeptides
- Polymers built from amino acids
- Make up proteins
Amino acids
- Organic molecules w/ amino and carboxyl groups
- R groups/ side chains make them differ in properties
- Linked by covalent peptide bonds
- Carboxyl end (C-terminus) and Amino end (N-terminus)
Four levels of Protein Structure
- Primary
- Secondary
- Tertiary
- Quaternary
Primary
- Unique sequence of amino acids
- Like order of letters in long word (order matters)
- Determined by inherited genetic info
Secondary
- Consists of coils and folds in polypeptide chain
- Result from hydrogen bonds between repeating parts of the polypeptide backbone
- A helix (coil) and B pleated sheet
Tertiary
- Determined by interactions among various side chains ( R groups)
- Interactions: hydrogen bonds, ionic bonds, hydrophobic interactions, and van der waals
- Disulfide bridges= strong covalent bonds that reinforce structure
Quaternary
- Protein consists of multiple polypeptide chains
- Ex: collagen, hemoglobin
What determines protein structure?
- Primary structure, pH, salt concentration, temp, environment
- Loss of native structure= denaturation
- Biologically inactive
Cells
- Fundamental units of life
- Simplest collection of matter that can be alive
- Studied using microscopes
Light Microscope (LM)
-Visible light passed through a specimen and glass lens
Magnification
-The ratio of an object’s image size to its real size (due to lens)
Resolution
-The measure of the clarity of the image, or the minimum distance between two distinguishable points
Contrast
-Visible differences in brightness between parts of the sample (between colors)
Electron microscopes
- Used to study subcellular structures
- Types: scanning electron microscopes (SEMs) and Transmission electron microscopes (TEMs)
- SEMs: Focus beam of electrons onto surface of specimen 3D
- TEMs: focus beam of electrons through specimen, internal structure
Cell fractionation
- Take cell apart and separate into organelles
- Uses centrifuge and diff speeds
- Heaviest is separating using low speed and vice versa
- Heaviest: Nuclei and cell debris
- Lightest: Ribosomes
Eukaryotic Cells
- Cells that have a nucleus (DNA) and membrane-enclosed organelles
- Membranes= lipid bilayer
- plants of chloroplasts, animals do not
- Ex: protists, fungi, animals, plants
Prokaryotic Cells
- Cell that does not have membrane-enclosed organelles, only a cell membrane and DNA
- Ex: Bacteria and Archaea
Nucleus
- Contains the cell’s genes
- Enclosed by the nuclear envelope (lipid bilayer), separates it from cytoplasm
- Lined w/ pores (regulate entry and exit of molecules from the nucleus)
- Nuclear Lamina: maintain its shape
Chromatin
- One DNA molecule in a chromosome
- Condenses to form chromosomes
Nucleolus
- Located within the nucleus
- Site of ribosomal RNA (rRNA) synthesis
Ribosomes
- Made of rRNA (ribosomal RNA) and protein
- Carry out protein synthesis in:
- Cytosol (free ribosomes)
- Outside ER or nuclear envelope (bound ribosomes)
Endoplasmic Reticulum
- Biosynthetic factory
- Continuous w/ nuclear envelope
- Regions: Smooth ER (no ribosomes) and Rough ER (studded w/ ribosomes)
Smooth ER
- Synthesizes lipids
- Metabolizes carbohydrates
- Detoxifies drugs and poisons
- Stores calcium ions
Rough ER
- Bound ribosomes that secrete glycoproteins
- Distributes transport vesicles, secretory proteins surrounded by membranes
- Membrane factory for the cell