2. Molecular Biology Flashcards
2.1 What is an organic compound?
Has carbon, found in living things
2.1 What are the bond properties of carbon compounds?
1) Carbon atoms form 2 covalent bonds with other atoms
2) Carbon atoms can form up to 4 nonpolar covalent bonds: allows for complex structure
2.1 Four Main Functional Groups
Hydroxyl (OH)
Amine (NH2)
Carboxyl (COOH)
Methyl (CH3)
2.1 What are the identifying features of carbohydrates?
1) Composed of C,H,O with a 2:1 of H:O
2) End in -ose
3) Many hydroxide groups
2.1 Draw ribose and glucose molecules
2.1 Classification of Carbohydrates
Monosaccharide: Monomer, soluble in water
Disaccharide: two monosaccharides
Oligiosaccharide: 3-10 monosaccharides
Polysaccharide: Lots of saccharides, energy storage or cell structure
2.1 Condensation vs hydrolosis
Condensation: Molecules form a covalent bond with water as a waste product
Hydrolosis: The opposite of condensation
2.1 Classes of Lipids
Monomers:
Fatty acids, monoglyceride
Polymer (ex)
Triglyceride
2.1 Basic info of Lipids
- Insoluble,hydrophobic
- A chain of hydrocarbons
- Fatty acids or a derivative
2.1 Common Lipids
Triglyceride: 3 fatty acids bonded to glyceral
Wax: long chain of hydrocarbons
Phospholipid
Steriods
2.1 Basic Structure of Protien
-Composed of at least one chain of amino acids
- Amino acids contain C,O,H,N with some containing S
Acids –> Polypeptide –> Protien
2.1 Classes of nucleic acid
Monomer:
Nucleotide
Polymer:
DNA
2.1 Basics of Nucleic Acids
- Chain of nucleotides
- Nucleotides contain C,H,O,N,P
- Nucleotide: Phosphate group attached to carbohydrate (deoxyribose or ribose) and nitrogeneous base
Ex: ATP, DNA
2.1 What is vitalism
The doctrine that organic molecules could only be syntehsized by living systems, disproved when urea was synthesized
2.1 Anabolism and Catabolism
Anabolism: Reactions that build, require ATP
Catabolism: broke down, release energy
2.2 Hydrogen Bonding Properties
1) Intramolecular polar covalent bonds between H+ and O-
2) Hydrogen bonds give water unique properties
2.2 Properties of Water
Cohesive: Water sticks to eachother
Adhesive: Water sticks to other polar + ionic molecules
Thermal Properties: Takes a lot of energy to change, high specific heat, high latent heat of vaporazation, high boiling point
Solvent: is a good solvent
2.2 Hydrophobic or Hydrophillic
Hydrophobic: no (+) or (-) charges, lipids,
Hydrophillic: Soluble
2.2 Transport in Blood Plasma
Sodium Chloride: Ionic compound, soluble
Amino Acid: + and -, some phillic some phobic soluble enough
Glucose: soluble in water, polar
Oxygen: nonpolar, small enough to disolve in water
Fat Molecules: non polar, large, carried in lipoprotien complexes
Cholestoral: hydrophobic, transported in lipoprotien complex
2.3 What are the common disaccharides
Lactose
Sucrose
Maltose
2.3 What are the common polysaccharides?
Cellulose - plant support (B-glucose)
Starch - plant storage (a-glucose), amylose - 1-4 bonds
amylopectin - 1-4 and 1-6 bonds
Glycogen - animal storage (a-glucose), 1-4 and 1-6 bonds
2.3 Common Monosaccharides
Glucose
Fructose
Galactose
2.3 Draw and label a fatty acid
2.3 Function of Lipids
cell membrane, hormones, nutrition, energy storage (harder to access), thermal insulation
2.3 Saturated v Unsaturated Fat
Saturated: No Double Bond
Unsaturated: double bound
Cis-unsaturated: H on same side, causes a kink
Trans-unsaturated: H on different sides, not found in nature
2.3 Purpose and structure of triglycerides
Long-term energy storage (fats in animals) (oil in plants(
Condensation reaction between one glycerol and three fatty acids
2.3 Health risk of lipid types
UnSaturated/Trans - raise LDL levels, raising cholestoral
Saturated - increases HDL levels, lowering cholestoral
2.3 HDL vs LDL
Low-densiriy lipoprotiens: carry cholestoral from liver to rest
High-densiity lipoprotien - scavenge excess cholestoral and bring back to liver
2.4 Draw the formation of a peptide bond
2.4 Draw and lable an amino acid
2.4 Amino Acids Structure
Composed of amine group (HxN), carboxyl group (CO2) and unique R-group with a H atom on top, central carbon atom
2.4 What is a proteome?
All of the protiens produed by a cell, tissue, or organism.
2.4 What is denaturation?
Disruption in the secondary, tertiary, or quaterny structure of a protien.
Caused by ^ in pH, temperature, chemicals
2.4 What is Rubisco?
An enzyme involved with the first step of carbon fixation
2.4 What is Insulin?
A protien that regulates blood sugar levels, signals to cells to take in glucose
2.4 What is immunoglobulin?
Antibodies
2.4 What is Rhodopsin?
A pigment that acts as a photorecepter in rod cells of retina
2.4 What is collagen?
A protien that provides structure for the body
2.4 Function of protiens
S- tructure
H- ormones
I- mmune
T- ransport
S- ensation
M- ovement
E- nzymes
2.4 What are the levels of protien structure?
Primary: Chain of amino acids, held by peptide bonds
Secondary: Hydrogen bonding leads to either alpha helix or pleated sheet
Tertiary: 3-D folding due to side chain interactions
Quaternary: More than one amino acid chain
2.5 What is the purpose of enzymes?
Speed up chemical reactions without being altered (catalyst)
2.5 Structure of enzymes
Enzymes have an active site that is specific to the substrate that binds to them. They convert the substrate into a product.
2.5 Draw and Label a graph showing the effects of Enzyme activity
2.5 Factors affecting enzyme activity
Temperature: High temperature = more collisions, more EA
But too high is denaturation
pH: Most enzymes have an optimal pH, any deviation leads to less EA
Substrate concentration: More substrate = more EA until too many active sites are blocked
2.6 Draw and label DNA
2.6 DNA vs RNA
Rna is made from ribose, DNA is made from deoxyribose
2.6 What’s the difference between Purine and Pyrimidine bases? Which are which?
Purine is larger with a doubel carbon ring: Guanine, Adenine
Pyrimidine has only a single carbon ring: Cytosine, Uracil, Thymine
2.7 What are codons
Three bases on mRNA that code for a aminoacid
2.7 What is PCR?
Polymerase Chain Reaction is a method of reproducing DNA in a lab
1) Denaturation - DNA is heated to seperate strands
2) Annealing - Sample is cooled so primers anneal
3) Elongation - sample is heated to optimal temperature for Taq primase
2.7 What is the difference between replication in Prokaryotes vs Eukaryotes?
Prokaryotes have 1 origin, 1 bubble, 2 forks
Eukaryotes have multiple origins that fuse
2.8 Write the basic formula for cellular respiration
C6H12O6 + 6 O2 (ADP+P) –> 6 CO2 + 6 H20 (+ATP)
2.8 Why must cells continue to respirate, features of ATP?
1) ATP can’t be stored
2) ATP can’t be transfered between cells
3) When ATP is used, heat energy is lost
2.8 What are the three major processes that glucose undertakes for cellular respiration?
Glycosis, Krebs Cycle, Electron Transport Chain
2.8 What is Anaerobic Respiration?
Anaerobic: No oxygen, back up when cellular oxygen is needed. ATP is needed quick. Allows microbes to live in oxygen-poor environments
2.8 Human v. Yeast Anaerobic Respiration
Yeast: Glycosis then alc fermentation (pyruvate –> ethanol)
Humans: Glycosis then lactic acid fermentation (pyruvate –> lactic acid)
2.8 Net ATP Anaerobic vs Aerobic
Ana : 2 per gluc
Aero: 38 per gluc
2.9 What is the formula for photosynthesis?
6 CO2 + 6 H20 –> C6H12O6 + 6 O2
2.9 What is photosynthesis?
The process of phototropic organisms converting light energy into glucose
2.9 Properties of Wavelengths
Shorter wave lengths = more energy,
Visible light: 380-700 (violet > red)
2.9 Why are plants green?
Chlorophyll, the main pigment of plants, absorbs red/blue light but reflects green light
2.9 What is the formula for light dependent reaction?
2 H2O –> 4 H (becomes NADH) + 4 e- (used for next part) + O2
2.9 What is the calvin cycle?
The light independent portion of photosynthesis in which Carbon, form CO2 is used to build carbohydrates, relies on ATP, NADH
2.9 Where do the light independent vs light independent reactions happen?
Dependent: thylakoid
Independent: Cytoplasm of chloroplast (stroma)
